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Zinc in PDB 3ave: Crystal Structure of the Fucosylated Fc Fragment From Human Immunoglobulin G1

Protein crystallography data

The structure of Crystal Structure of the Fucosylated Fc Fragment From Human Immunoglobulin G1, PDB code: 3ave was solved by S.Matsumiya, Y.Yamaguchi, J.Saito, M.Nagano, H.Sasakawa, S.Otaki, M.Satoh, K.Shitara, K.Kato, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.72 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.419, 78.471, 143.758, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 23.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Fucosylated Fc Fragment From Human Immunoglobulin G1 (pdb code 3ave). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Fucosylated Fc Fragment From Human Immunoglobulin G1, PDB code: 3ave:

Zinc binding site 1 out of 1 in 3ave

Go back to Zinc Binding Sites List in 3ave
Zinc binding site 1 out of 1 in the Crystal Structure of the Fucosylated Fc Fragment From Human Immunoglobulin G1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Fucosylated Fc Fragment From Human Immunoglobulin G1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn448

b:34.0
occ:1.00
O A:HOH457 2.0 32.3 1.0
ND1 A:HIS268 2.1 34.4 1.0
O A:HOH458 2.2 36.7 1.0
CG A:HIS268 3.1 36.5 1.0
CE1 A:HIS268 3.2 34.3 1.0
CB A:HIS268 3.4 37.1 1.0
CD2 A:HIS268 4.3 34.3 1.0
NE2 A:HIS268 4.3 33.9 1.0
C A:HIS268 4.4 38.3 1.0
O A:HIS268 4.5 38.0 1.0
CA A:HIS268 4.5 37.1 1.0
N A:GLU269 4.7 39.8 1.0

Reference:

S.Matsumiya, Y.Yamaguchi, J.Saito, M.Nagano, H.Sasakawa, S.Otaki, M.Satoh, K.Shitara, K.Kato. Corrigendum to "Structural Comparison of Fucosylated and Nonfucosylated Fc Fragments of Human Immunoglobulin G1" [J. Mol. Biol. 386/3 (2007) 767-779] J.Mol.Biol. V. 408 1001 2011.
ISSN: ISSN 0022-2836
DOI: 10.1016/J.JMB.2011.03.031
Page generated: Thu Oct 24 11:17:52 2024

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