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Zinc in PDB 2ql1: Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment

Protein crystallography data

The structure of Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment, PDB code: 2ql1 was solved by V.Oganesyan, H.Wu, W.F.Dall'acqua, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.25 / 2.53
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 49.869, 147.492, 74.315, 90.00, 90.00, 90.00
R / Rfree (%) 23.2 / 29.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment (pdb code 2ql1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment, PDB code: 2ql1:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2ql1

Go back to Zinc Binding Sites List in 2ql1
Zinc binding site 1 out of 4 in the Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:52.5
occ:1.00
NE2 A:HIS310 1.9 22.8 1.0
NE2 A:HIS435 2.0 30.9 1.0
O A:HOH451 2.5 38.4 1.0
O A:HOH458 2.6 48.5 1.0
CE1 A:HIS310 2.8 23.2 1.0
CD2 A:HIS310 2.9 22.0 1.0
CD2 A:HIS435 3.0 29.6 1.0
CE1 A:HIS435 3.0 27.8 1.0
CD1 A:LEU314 3.7 35.0 1.0
ND1 A:HIS310 4.0 22.1 1.0
CG A:HIS310 4.0 25.8 1.0
ND1 A:HIS435 4.1 25.9 1.0
CG A:HIS435 4.1 26.7 1.0

Zinc binding site 2 out of 4 in 2ql1

Go back to Zinc Binding Sites List in 2ql1
Zinc binding site 2 out of 4 in the Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2

b:83.1
occ:0.50
NE2 A:HIS433 2.3 25.6 1.0
CE1 A:HIS433 2.8 23.0 1.0
CD2 A:HIS433 3.5 24.9 1.0
ND1 A:HIS433 4.1 21.2 1.0
ND2 A:ASN434 4.2 23.3 1.0
CG A:HIS433 4.4 23.2 1.0
CG A:ASN434 4.9 23.4 1.0
OD1 A:ASN434 4.9 22.6 1.0

Zinc binding site 3 out of 4 in 2ql1

Go back to Zinc Binding Sites List in 2ql1
Zinc binding site 3 out of 4 in the Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn3

b:61.2
occ:0.50
O A:HOH465 1.9 53.3 1.0
OE2 A:GLU318 2.3 42.6 1.0
OE1 A:GLU318 2.7 40.2 1.0
CD A:GLU318 2.8 39.0 1.0
CG A:GLU318 4.2 37.1 1.0
CG2 A:THR335 4.3 41.7 1.0
CB A:GLU318 4.9 36.1 1.0
CB A:THR335 4.9 41.5 1.0

Zinc binding site 4 out of 4 in 2ql1

Go back to Zinc Binding Sites List in 2ql1
Zinc binding site 4 out of 4 in the Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4

b:0.1
occ:1.00
OE1 A:GLU345 2.3 38.1 1.0
CD A:GLU345 2.8 35.9 1.0
OE2 A:GLU345 2.8 41.8 1.0
O A:HOH453 2.8 64.6 1.0
N A:HIS433 3.9 24.8 1.0
CG A:GLU345 4.1 33.9 1.0
CB A:HIS433 4.2 22.8 1.0
CA A:HIS433 4.6 23.9 1.0
O A:ALA431 4.6 27.6 1.0
CA A:LEU432 4.7 24.1 1.0
C A:LEU432 4.7 24.3 1.0
CD2 A:LEU432 5.0 17.4 1.0

Reference:

V.Oganesyan, M.M.Damschroder, W.Leach, H.Wu, W.F.Dall'acqua. Structural Characterization of A Mutated, Adcc-Enhanced Human Fc Fragment Mol.Immunol. V. 45 1872 2008.
ISSN: ISSN 0161-5890
PubMed: 18078997
DOI: 10.1016/J.MOLIMM.2007.10.042
Page generated: Thu Oct 17 03:29:32 2024

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