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Cobalt in PDB 1k98: Adomet Complex of Meth C-Terminal Fragment

Enzymatic activity of Adomet Complex of Meth C-Terminal Fragment

All present enzymatic activity of Adomet Complex of Meth C-Terminal Fragment:
2.1.1.13;

Protein crystallography data

The structure of Adomet Complex of Meth C-Terminal Fragment, PDB code: 1k98 was solved by V.Bandarian, K.A.Pattridge, B.W.Lennon, D.P.Huddler, R.G.Matthews, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 3.75
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 108.503, 108.503, 146.474, 90.00, 90.00, 90.00
R / Rfree (%) 30.8 / 36.3

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Adomet Complex of Meth C-Terminal Fragment (pdb code 1k98). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Adomet Complex of Meth C-Terminal Fragment, PDB code: 1k98:

Cobalt binding site 1 out of 1 in 1k98

Go back to Cobalt Binding Sites List in 1k98
Cobalt binding site 1 out of 1 in the Adomet Complex of Meth C-Terminal Fragment


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Adomet Complex of Meth C-Terminal Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1248

b:89.1
occ:1.00
CO A:B121248 0.0 89.1 1.0
N23 A:B121248 1.9 89.6 1.0
N21 A:B121248 2.0 90.3 1.0
N22 A:B121248 2.0 88.5 1.0
N24 A:B121248 2.1 94.5 1.0
C11 A:B121248 3.0 89.4 1.0
C9 A:B121248 3.0 87.6 1.0
C1 A:B121248 3.0 91.4 1.0
C4 A:B121248 3.0 89.8 1.0
C19 A:B121248 3.1 92.1 1.0
C14 A:B121248 3.2 89.9 1.0
C6 A:B121248 3.2 88.6 1.0
C16 A:B121248 3.3 92.6 1.0
C10 A:B121248 3.4 87.7 1.0
C5 A:B121248 3.5 89.0 1.0
C20 A:B121248 3.6 89.6 1.0
C15 A:B121248 3.8 92.0 1.0
OH A:TYR1139 4.0 89.5 1.0
C12 A:B121248 4.2 88.3 1.0
C13 A:B121248 4.3 91.0 1.0
C2 A:B121248 4.4 92.6 1.0
C3 A:B121248 4.4 92.8 1.0
C18 A:B121248 4.4 93.0 1.0
C8 A:B121248 4.4 86.1 1.0
C7 A:B121248 4.4 86.6 1.0
C17 A:B121248 4.6 92.5 1.0
C46 A:B121248 4.7 88.0 1.0
C41 A:B121248 4.8 86.9 1.0
CZ A:TYR1139 4.9 88.7 1.0
C35 A:B121248 4.9 90.5 1.0
C37 A:B121248 5.0 84.3 1.0

Reference:

V.Bandarian, K.A.Pattridge, B.W.Lennon, D.P.Huddler, R.G.Matthews, M.L.Ludwig. Domain Alternation Switches B(12)-Dependent Methionine Synthase to the Activation Conformation. Nat.Struct.Biol. V. 9 53 2002.
ISSN: ISSN 1072-8368
PubMed: 11731805
DOI: 10.1038/NSB738
Page generated: Sun Jul 13 17:37:26 2025

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