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Cobalt in PDB 8sse: Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8

Enzymatic activity of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8

All present enzymatic activity of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8:
2.1.1.13;

Protein crystallography data

The structure of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8, PDB code: 8sse was solved by K.Yamada, J.Mendoza, M.Koutmos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.30 / 3.15
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 166.135, 95.844, 238.745, 90, 91.96, 90
R / Rfree (%) 24.5 / 30.7

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8 (pdb code 8sse). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 6 binding sites of Cobalt where determined in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8, PDB code: 8sse:
Jump to Cobalt binding site number: 1; 2; 3; 4; 5; 6;

Cobalt binding site 1 out of 6 in 8sse

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Cobalt binding site 1 out of 6 in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1201

b:48.7
occ:1.00
CO A:B121201 0.0 48.7 1.0
N24 A:B121201 1.9 48.3 1.0
N23 A:B121201 1.9 50.2 1.0
N21 A:B121201 1.9 45.1 1.0
N22 A:B121201 1.9 51.7 1.0
C9 A:B121201 2.8 53.7 1.0
C19 A:B121201 2.8 48.7 1.0
C16 A:B121201 2.9 47.9 1.0
C1 A:B121201 2.9 45.0 1.0
C14 A:B121201 2.9 49.1 1.0
C4 A:B121201 2.9 43.9 1.0
C11 A:B121201 2.9 51.8 1.0
C6 A:B121201 3.0 46.4 1.0
C10 A:B121201 3.2 54.2 1.0
C15 A:B121201 3.3 47.1 1.0
C5 A:B121201 3.3 44.1 1.0
C20 A:B121201 3.5 46.8 1.0
OH A:TYR1132 3.9 60.8 1.0
C8 A:B121201 4.0 49.6 1.0
C18 A:B121201 4.1 50.2 1.0
C2 A:B121201 4.1 46.0 1.0
C13 A:B121201 4.1 55.0 1.0
C41 A:B121201 4.1 49.9 1.0
C3 A:B121201 4.2 46.5 1.0
C17 A:B121201 4.2 48.7 1.0
C12 A:B121201 4.2 52.4 1.0
C7 A:B121201 4.2 48.2 1.0
O A:HOH1312 4.4 30.7 1.0
C26 A:B121201 4.5 46.7 1.0
C48 A:B121201 4.5 68.3 1.0
C35 A:B121201 4.7 47.0 1.0
C53 A:B121201 4.7 49.6 1.0
C54 A:B121201 4.7 47.3 1.0
CZ A:TYR1132 4.8 56.0 1.0
C37 A:B121201 4.9 50.3 1.0
C46 A:B121201 4.9 53.7 1.0
CE2 A:TYR1132 4.9 64.3 1.0

Cobalt binding site 2 out of 6 in 8sse

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Cobalt binding site 2 out of 6 in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co1201

b:77.9
occ:1.00
CO B:B121201 0.0 77.9 1.0
N23 B:B121201 1.8 78.6 1.0
N21 B:B121201 1.9 68.2 1.0
N24 B:B121201 1.9 79.5 1.0
N22 B:B121201 1.9 77.7 1.0
C9 B:B121201 2.8 80.0 1.0
C14 B:B121201 2.8 77.9 1.0
C11 B:B121201 2.8 91.0 1.0
C19 B:B121201 2.9 73.2 1.0
C1 B:B121201 2.9 65.8 1.0
C4 B:B121201 2.9 63.8 1.0
C16 B:B121201 2.9 79.1 1.0
C6 B:B121201 3.0 66.0 1.0
O B:HOH1315 3.1 42.1 1.0
C10 B:B121201 3.2 84.9 1.0
C15 B:B121201 3.3 74.3 1.0
C5 B:B121201 3.3 58.2 1.0
C20 B:B121201 3.5 58.7 1.0
O B:HOH1326 3.7 36.7 1.0
C13 B:B121201 4.0 93.4 1.0
C8 B:B121201 4.0 71.7 1.0
C2 B:B121201 4.1 77.2 1.0
C18 B:B121201 4.1 76.2 1.0
C12 B:B121201 4.2 98.8 1.0
C3 B:B121201 4.2 70.6 1.0
OH B:TYR1132 4.2 92.3 1.0
C17 B:B121201 4.2 73.6 1.0
C41 B:B121201 4.2 77.6 1.0
C7 B:B121201 4.2 71.7 1.0
C48 B:B121201 4.3 96.2 1.0
C26 B:B121201 4.4 94.7 1.0
C35 B:B121201 4.7 56.3 1.0
C54 B:B121201 4.7 64.5 1.0
C53 B:B121201 4.7 70.9 1.0
C37 B:B121201 4.9 78.6 1.0
C46 B:B121201 4.9 96.7 1.0
CZ B:TYR1132 4.9 75.1 1.0
C42 B:B121201 5.0 76.2 1.0

Cobalt binding site 3 out of 6 in 8sse

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Cobalt binding site 3 out of 6 in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Co1201

b:48.2
occ:1.00
CO C:B121201 0.0 48.2 1.0
N21 C:B121201 1.8 47.1 1.0
N23 C:B121201 1.9 46.4 1.0
N24 C:B121201 1.9 49.4 1.0
N22 C:B121201 1.9 50.4 1.0
C19 C:B121201 2.8 49.9 1.0
C9 C:B121201 2.8 51.2 1.0
C4 C:B121201 2.8 46.1 1.0
C14 C:B121201 2.9 47.0 1.0
C1 C:B121201 2.9 48.8 1.0
C11 C:B121201 2.9 47.5 1.0
C16 C:B121201 2.9 46.0 1.0
C6 C:B121201 3.0 44.8 1.0
C10 C:B121201 3.2 49.6 1.0
C5 C:B121201 3.3 42.5 1.0
C15 C:B121201 3.3 43.2 1.0
C20 C:B121201 3.6 46.2 1.0
C18 C:B121201 4.1 50.5 1.0
C8 C:B121201 4.1 50.6 1.0
C13 C:B121201 4.1 53.0 1.0
C2 C:B121201 4.1 53.0 1.0
C3 C:B121201 4.1 52.7 1.0
C17 C:B121201 4.2 49.3 1.0
C12 C:B121201 4.2 48.1 1.0
C7 C:B121201 4.3 47.8 1.0
C48 C:B121201 4.4 63.8 1.0
O C:HOH1326 4.4 27.1 1.0
C41 C:B121201 4.4 51.6 1.0
OH C:TYR1132 4.5 53.4 1.0
C26 C:B121201 4.5 57.2 1.0
C35 C:B121201 4.7 42.1 1.0
C54 C:B121201 4.7 51.4 1.0
C53 C:B121201 4.7 41.5 1.0
C46 C:B121201 4.8 47.6 1.0
CE1 C:TYR1132 4.9 54.0 1.0
C42 C:B121201 4.9 51.9 1.0
C37 C:B121201 5.0 51.7 1.0

Cobalt binding site 4 out of 6 in 8sse

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Cobalt binding site 4 out of 6 in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 4 of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Co1201

b:69.1
occ:1.00
CO D:B121201 0.0 69.1 1.0
N23 D:B121201 1.9 75.7 1.0
N21 D:B121201 1.9 67.5 1.0
N24 D:B121201 1.9 82.7 1.0
N22 D:B121201 1.9 70.8 1.0
C9 D:B121201 2.8 68.1 1.0
C14 D:B121201 2.8 87.2 1.0
C19 D:B121201 2.8 79.8 1.0
C11 D:B121201 2.8 79.9 1.0
C1 D:B121201 2.8 72.3 1.0
C16 D:B121201 2.9 84.9 1.0
C4 D:B121201 2.9 64.1 1.0
C6 D:B121201 3.0 61.0 1.0
C10 D:B121201 3.1 70.7 1.0
C15 D:B121201 3.3 83.2 1.0
C20 D:B121201 3.3 66.5 1.0
C5 D:B121201 3.4 56.7 1.0
C48 D:B121201 3.6 112.0 1.0
C13 D:B121201 3.8 103.7 1.0
C12 D:B121201 4.0 103.0 1.0
C18 D:B121201 4.1 87.3 1.0
C8 D:B121201 4.1 65.5 1.0
C2 D:B121201 4.1 74.6 1.0
OH D:TYR1132 4.1 81.3 1.0
C17 D:B121201 4.2 81.7 1.0
C3 D:B121201 4.2 71.0 1.0
C7 D:B121201 4.2 62.0 1.0
C26 D:B121201 4.6 76.9 1.0
C54 D:B121201 4.6 77.5 1.0
C35 D:B121201 4.7 53.7 1.0
C53 D:B121201 4.7 84.8 1.0
C37 D:B121201 4.8 60.2 1.0
C46 D:B121201 4.9 108.1 1.0
C41 D:B121201 4.9 66.8 1.0

Cobalt binding site 5 out of 6 in 8sse

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Cobalt binding site 5 out of 6 in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 5 of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Co1201

b:40.1
occ:1.00
CO E:B121201 0.0 40.1 1.0
N23 E:B121201 1.8 45.9 1.0
N24 E:B121201 1.9 45.7 1.0
N22 E:B121201 1.9 41.9 1.0
N21 E:B121201 1.9 42.7 1.0
C9 E:B121201 2.8 41.8 1.0
C19 E:B121201 2.8 45.9 1.0
C11 E:B121201 2.8 49.2 1.0
C14 E:B121201 2.9 47.0 1.0
C16 E:B121201 2.9 46.6 1.0
C1 E:B121201 2.9 44.1 1.0
C4 E:B121201 3.0 41.2 1.0
C6 E:B121201 3.0 39.6 1.0
C10 E:B121201 3.1 45.3 1.0
C15 E:B121201 3.3 43.2 1.0
C5 E:B121201 3.4 37.3 1.0
C20 E:B121201 3.5 42.2 1.0
C8 E:B121201 4.0 40.3 1.0
C18 E:B121201 4.1 49.2 1.0
C13 E:B121201 4.1 55.5 1.0
C12 E:B121201 4.1 55.2 1.0
C17 E:B121201 4.2 48.2 1.0
C2 E:B121201 4.2 51.6 1.0
C7 E:B121201 4.2 40.3 1.0
C3 E:B121201 4.3 46.1 1.0
C41 E:B121201 4.3 41.6 1.0
OH E:TYR1132 4.3 63.7 1.0
O E:HOH1302 4.4 23.0 1.0
C48 E:B121201 4.5 58.9 1.0
C26 E:B121201 4.6 60.6 1.0
C53 E:B121201 4.7 42.3 1.0
C35 E:B121201 4.7 36.8 1.0
C54 E:B121201 4.8 45.9 1.0
C46 E:B121201 4.9 52.5 1.0
C37 E:B121201 4.9 42.7 1.0
CE1 E:TYR1132 4.9 58.5 1.0
CZ E:TYR1132 5.0 54.0 1.0

Cobalt binding site 6 out of 6 in 8sse

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Cobalt binding site 6 out of 6 in the Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 6 of Methionine Synthase, C-Terminal Fragment, Cobalamin and Reactivation Domains From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Co1201

b:69.0
occ:1.00
CO F:B121201 0.0 69.0 1.0
N23 F:B121201 1.9 86.8 1.0
N21 F:B121201 1.9 79.7 1.0
N22 F:B121201 1.9 71.3 1.0
N24 F:B121201 1.9 75.7 1.0
C9 F:B121201 2.8 76.5 1.0
C19 F:B121201 2.8 80.9 1.0
C11 F:B121201 2.9 88.8 1.0
C4 F:B121201 2.9 70.6 1.0
C1 F:B121201 2.9 73.4 1.0
C14 F:B121201 2.9 81.3 1.0
C6 F:B121201 2.9 71.5 1.0
C16 F:B121201 2.9 75.4 1.0
C10 F:B121201 3.2 89.4 1.0
C5 F:B121201 3.3 59.6 1.0
C15 F:B121201 3.4 78.5 1.0
C20 F:B121201 3.5 65.3 1.0
OH F:TYR1132 3.9 90.9 1.0
C8 F:B121201 4.1 69.8 1.0
C13 F:B121201 4.1 88.7 1.0
C18 F:B121201 4.1 83.7 1.0
C2 F:B121201 4.1 76.8 1.0
C3 F:B121201 4.2 74.7 1.0
C12 F:B121201 4.2 92.0 1.0
O F:HOH1330 4.2 34.4 1.0
C7 F:B121201 4.2 78.9 1.0
C17 F:B121201 4.2 77.1 1.0
C48 F:B121201 4.4 92.2 1.0
C26 F:B121201 4.4 78.9 1.0
C35 F:B121201 4.6 56.1 1.0
CZ F:TYR1132 4.8 82.6 1.0
C41 F:B121201 4.8 64.8 1.0
C53 F:B121201 4.8 80.4 1.0
C46 F:B121201 4.8 92.2 1.0
C37 F:B121201 4.9 80.0 1.0
CE2 F:TYR1132 4.9 84.9 1.0
C54 F:B121201 4.9 69.2 1.0

Reference:

J.Mendoza, M.Purchal, K.Yamada, M.Koutmos. Structure of Full-Length Cobalamin-Dependent Methionine Synthase and Cofactor Loading Captured in Crystallo Biorxiv 2023.
ISSN: ISSN 2692-8205
DOI: 10.1101/2023.06.15.544998
Page generated: Tue Jul 30 20:03:36 2024

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