Atomistry » Zinc » PDB 2q38-2qm1 » 2ql1
Atomistry »
  Zinc »
    PDB 2q38-2qm1 »
      2ql1 »

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

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy