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Cobalt in PDB 4zrq: E88 Deletion Mutant of CD320 in Complex with TC2

Protein crystallography data

The structure of E88 Deletion Mutant of CD320 in Complex with TC2, PDB code: 4zrq was solved by A.Alam, K.P.Locher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.43 / 2.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 98.404, 98.404, 356.341, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 23.1

Other elements in 4zrq:

The structure of E88 Deletion Mutant of CD320 in Complex with TC2 also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the E88 Deletion Mutant of CD320 in Complex with TC2 (pdb code 4zrq). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the E88 Deletion Mutant of CD320 in Complex with TC2, PDB code: 4zrq:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 4zrq

Go back to Cobalt Binding Sites List in 4zrq
Cobalt binding site 1 out of 2 in the E88 Deletion Mutant of CD320 in Complex with TC2


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of E88 Deletion Mutant of CD320 in Complex with TC2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co501

b:72.2
occ:1.00
CO A:CNC501 0.0 72.2 1.0
N24 A:CNC501 1.7 54.3 0.5
N21 A:CNC501 1.8 74.9 1.0
N22 A:CNC501 1.8 71.0 1.0
N23 A:CNC501 1.9 61.7 1.0
C1A A:CNC501 2.1 69.6 0.5
C19 A:CNC501 2.6 47.6 1.0
N3B A:CNC501 2.7 32.8 1.0
C9 A:CNC501 2.7 60.4 1.0
C1 A:CNC501 2.7 64.9 1.0
C11 A:CNC501 2.8 58.6 1.0
C16 A:CNC501 2.9 55.7 1.0
C6 A:CNC501 2.9 71.9 1.0
C4 A:CNC501 2.9 79.2 0.5
C14 A:CNC501 3.0 60.1 0.5
N1A A:CNC501 3.3 74.3 1.0
C5 A:CNC501 3.4 34.5 1.0
C10 A:CNC501 3.4 34.8 1.0
C15 A:CNC501 3.4 52.4 1.0
C2B A:CNC501 3.6 34.7 1.0
C26 A:CNC501 3.7 34.4 1.0
C20 A:CNC501 3.7 32.5 0.8
C9B A:CNC501 3.7 32.8 0.8
C18 A:CNC501 3.7 41.3 1.0
C2 A:CNC501 3.9 54.4 0.7
C17 A:CNC501 4.0 50.3 1.0
C3 A:CNC501 4.0 82.1 1.0
C8 A:CNC501 4.1 46.7 1.0
C4B A:CNC501 4.1 32.5 1.0
O A:HOH608 4.1 65.7 1.0
C12 A:CNC501 4.2 64.4 1.0
C7 A:CNC501 4.2 45.8 1.0
C13 A:CNC501 4.2 56.0 1.0
C30 A:CNC501 4.2 76.6 1.0
N1B A:CNC501 4.8 36.0 0.7
C35 A:CNC501 4.8 34.9 1.0
C53 A:CNC501 4.9 49.2 1.0
C8B A:CNC501 4.9 34.2 1.0
C41 A:CNC501 4.9 42.7 1.0
C47 A:CNC501 5.0 68.1 1.0

Cobalt binding site 2 out of 2 in 4zrq

Go back to Cobalt Binding Sites List in 4zrq
Cobalt binding site 2 out of 2 in the E88 Deletion Mutant of CD320 in Complex with TC2


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of E88 Deletion Mutant of CD320 in Complex with TC2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co501

b:68.7
occ:1.00
CO B:CNC501 0.0 68.7 1.0
N24 B:CNC501 1.7 62.6 0.5
N22 B:CNC501 1.8 83.0 1.0
N21 B:CNC501 1.9 84.2 1.0
N23 B:CNC501 1.9 84.0 1.0
C1A B:CNC501 2.1 59.6 0.5
C19 B:CNC501 2.6 55.6 1.0
N3B B:CNC501 2.7 38.7 1.0
C1 B:CNC501 2.7 76.0 1.0
C9 B:CNC501 2.9 63.4 0.6
C16 B:CNC501 2.9 57.0 1.0
C6 B:CNC501 2.9 91.3 1.0
C14 B:CNC501 2.9 78.7 0.7
C11 B:CNC501 3.0 86.9 0.6
C4 B:CNC501 3.0 80.5 0.5
N1A B:CNC501 3.3 56.3 1.0
C15 B:CNC501 3.4 52.1 1.0
C2B B:CNC501 3.4 37.7 1.0
C10 B:CNC501 3.4 41.2 1.0
C5 B:CNC501 3.4 45.0 1.0
C20 B:CNC501 3.7 38.7 0.9
C18 B:CNC501 3.7 46.1 1.0
C26 B:CNC501 3.7 43.9 1.0
C9B B:CNC501 3.8 39.4 0.9
C2 B:CNC501 3.9 69.2 1.0
C12 B:CNC501 3.9 58.5 1.0
C8 B:CNC501 4.0 46.5 1.0
C17 B:CNC501 4.0 48.1 1.0
C47 B:CNC501 4.1 62.3 1.0
C13 B:CNC501 4.2 72.2 1.0
C7 B:CNC501 4.2 46.5 0.9
C3 B:CNC501 4.2 76.5 1.0
C30 B:CNC501 4.2 74.1 1.0
C4B B:CNC501 4.3 40.6 1.0
C41 B:CNC501 4.5 41.7 1.0
N1B B:CNC501 4.7 38.2 0.7
C8B B:CNC501 4.8 40.2 1.0
C53 B:CNC501 4.9 48.5 1.0
C35 B:CNC501 4.9 47.4 1.0

Reference:

A.Alam, J.S.Woo, J.Schmitz, B.Prinz, K.Root, F.Chen, J.S.Bloch, R.Zenobi, K.P.Locher. Structural Basis of Transcobalamin Recognition By Human CD320 Receptor. Nat Commun V. 7 12100 2016.
ISSN: ESSN 2041-1723
PubMed: 27411955
DOI: 10.1038/NCOMMS12100
Page generated: Tue Jul 30 17:41:19 2024

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