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Zinc in PDB 2qla: Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules

Protein crystallography data

The structure of Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules, PDB code: 2qla was solved by F.A.Tezcan, E.N.Salgado, J.Faraone-Mennella, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 88.984, 66.659, 68.901, 90.00, 90.00, 90.00
R / Rfree (%) 24.8 / 29.5

Other elements in 2qla:

The structure of Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules (pdb code 2qla). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules, PDB code: 2qla:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2qla

Go back to Zinc Binding Sites List in 2qla
Zinc binding site 1 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


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 A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:22.2
occ:1.00
NE2 A:HIS73 2.1 28.6 1.0
NE2 A:HIS77 2.1 18.3 1.0
NE2 D:HIS63 2.2 25.8 1.0
OD2 C:ASP74 2.3 16.9 1.0
OD1 C:ASP74 2.5 14.5 1.0
CG C:ASP74 2.7 13.4 1.0
CD2 D:HIS63 2.8 24.5 1.0
CE1 A:HIS77 2.9 19.1 1.0
CE1 A:HIS73 3.1 33.1 1.0
CD2 A:HIS73 3.1 29.9 1.0
CD2 A:HIS77 3.3 22.1 1.0
CE1 D:HIS63 3.3 29.1 1.0
CG D:HIS63 4.0 28.3 1.0
ND1 A:HIS77 4.1 18.8 1.0
ND1 A:HIS73 4.2 32.2 1.0
CB C:ASP74 4.2 17.9 1.0
CG A:HIS73 4.2 27.8 1.0
ND1 D:HIS63 4.2 32.3 1.0
CG A:HIS77 4.3 21.4 1.0
CD1 D:ILE67 4.6 16.0 1.0
CD2 C:LEU78 4.7 21.9 1.0
O C:ASP74 4.7 18.8 1.0
CA C:ASP74 4.9 17.2 1.0

Zinc binding site 2 out of 4 in 2qla

Go back to Zinc Binding Sites List in 2qla
Zinc binding site 2 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn502

b:28.1
occ:1.00
NE2 B:HIS77 2.0 29.6 1.0
NE2 C:HIS63 2.0 30.4 1.0
OD2 D:ASP74 2.1 23.0 1.0
NE2 B:HIS73 2.2 26.5 1.0
OD1 D:ASP74 2.6 24.6 1.0
CG D:ASP74 2.7 21.9 1.0
CE1 B:HIS77 2.8 27.8 1.0
CE1 B:HIS73 2.9 29.4 1.0
CE1 C:HIS63 2.9 30.6 1.0
CD2 C:HIS63 3.1 32.8 1.0
CD2 B:HIS77 3.1 28.9 1.0
CD2 B:HIS73 3.4 26.9 1.0
CD1 C:ILE67 4.0 7.5 1.0
ND1 B:HIS77 4.0 24.6 1.0
ND1 C:HIS63 4.1 34.7 1.0
ND1 B:HIS73 4.1 29.8 1.0
CB D:ASP74 4.1 22.0 1.0
CG B:HIS77 4.2 27.4 1.0
CG C:HIS63 4.2 33.8 1.0
CG B:HIS73 4.4 27.4 1.0
CA D:ASP74 4.9 20.2 1.0
CG1 C:ILE67 4.9 15.4 1.0

Zinc binding site 3 out of 4 in 2qla

Go back to Zinc Binding Sites List in 2qla
Zinc binding site 3 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn501

b:20.2
occ:1.00
NE2 C:HIS73 2.0 29.6 1.0
NE2 C:HIS77 2.1 19.9 1.0
NE2 B:HIS63 2.2 24.9 1.0
OD2 A:ASP74 2.3 22.0 1.0
OD1 A:ASP74 2.5 21.5 1.0
CG A:ASP74 2.7 19.1 1.0
CE1 C:HIS73 2.8 29.0 1.0
CE1 C:HIS77 2.9 23.4 1.0
CD2 B:HIS63 2.9 23.0 1.0
CD2 C:HIS73 3.1 28.2 1.0
CD2 C:HIS77 3.2 23.4 1.0
CE1 B:HIS63 3.3 27.8 1.0
ND1 C:HIS73 4.0 29.3 1.0
ND1 C:HIS77 4.1 24.9 1.0
CG B:HIS63 4.2 26.9 1.0
CB A:ASP74 4.2 21.9 1.0
CG C:HIS73 4.2 26.9 1.0
CG C:HIS77 4.2 22.2 1.0
ND1 B:HIS63 4.3 26.4 1.0
CD1 B:ILE67 4.5 13.9 1.0
O A:ASP74 4.6 18.8 1.0
CD2 A:LEU78 4.7 32.0 1.0
CA A:ASP74 4.8 19.6 1.0
O A:HOH626 4.9 5.0 1.0

Zinc binding site 4 out of 4 in 2qla

Go back to Zinc Binding Sites List in 2qla
Zinc binding site 4 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn503

b:40.4
occ:1.00
NE2 D:HIS77 2.0 33.5 1.0
NE2 A:HIS63 2.0 28.9 1.0
OD2 B:ASP74 2.1 21.7 1.0
NE2 D:HIS73 2.3 26.4 1.0
OD1 B:ASP74 2.6 17.6 1.0
CG B:ASP74 2.7 17.8 1.0
CE1 D:HIS73 2.8 25.6 1.0
CE1 A:HIS63 2.9 23.2 1.0
CE1 D:HIS77 2.9 36.9 1.0
CD2 A:HIS63 3.1 28.5 1.0
CD2 D:HIS77 3.1 34.3 1.0
CD2 D:HIS73 3.5 27.8 1.0
CD1 A:ILE67 3.8 19.0 1.0
ND1 A:HIS63 4.0 27.0 1.0
ND1 D:HIS77 4.0 37.0 1.0
ND1 D:HIS73 4.1 29.1 1.0
CG A:HIS63 4.2 29.6 1.0
CG D:HIS77 4.2 33.6 1.0
CB B:ASP74 4.2 21.8 1.0
CG D:HIS73 4.5 26.0 1.0
CG1 A:ILE67 4.7 20.9 1.0
CA B:ASP74 5.0 22.8 1.0

Reference:

E.N.Salgado, J.Faraone-Mennella, F.A.Tezcan. Controlling Protein-Protein Interactions Through Metal Coordination: Assembly of A 16-Helix Bundle Protein. J.Am.Chem.Soc. V. 129 13374 2007.
ISSN: ISSN 0002-7863
PubMed: 17929927
DOI: 10.1021/JA075261O
Page generated: Wed Dec 16 03:50:37 2020

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