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Zinc in PDB 3uwb: Crystal Structure of A Probable Peptide Deformylase From Strucynechococcus Phage S-SSM7 in Complex with Actinonin

Protein crystallography data

The structure of Crystal Structure of A Probable Peptide Deformylase From Strucynechococcus Phage S-SSM7 in Complex with Actinonin, PDB code: 3uwb was solved by D.Lorimer, J.Abendroth, T.E.Edwards, A.Burgin, A.Segall, F.Rohwer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.62 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.810, 59.150, 61.460, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 17.1

Other elements in 3uwb:

The structure of Crystal Structure of A Probable Peptide Deformylase From Strucynechococcus Phage S-SSM7 in Complex with Actinonin also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Probable Peptide Deformylase From Strucynechococcus Phage S-SSM7 in Complex with Actinonin (pdb code 3uwb). 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 A Probable Peptide Deformylase From Strucynechococcus Phage S-SSM7 in Complex with Actinonin, PDB code: 3uwb:

Zinc binding site 1 out of 1 in 3uwb

Go back to Zinc Binding Sites List in 3uwb
Zinc binding site 1 out of 1 in the Crystal Structure of A Probable Peptide Deformylase From Strucynechococcus Phage S-SSM7 in Complex with Actinonin


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 Probable Peptide Deformylase From Strucynechococcus Phage S-SSM7 in Complex with Actinonin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn200

b:17.6
occ:1.00
NE2 A:HIS134 2.1 13.4 1.0
NE2 A:HIS138 2.1 14.3 1.0
O2 A:BB2154 2.1 15.5 1.0
O4 A:BB2154 2.2 19.3 1.0
SG A:CYS92 2.3 13.5 1.0
C3 A:BB2154 2.9 16.9 1.0
N1 A:BB2154 2.9 16.0 1.0
CD2 A:HIS134 3.0 12.6 1.0
CD2 A:HIS138 3.1 13.3 1.0
CE1 A:HIS134 3.1 13.5 1.0
CE1 A:HIS138 3.1 14.9 1.0
NE2 A:GLN49 3.3 14.0 1.0
CB A:CYS92 3.4 13.7 1.0
O A:HOH204 3.7 17.3 1.0
CA A:CYS92 3.8 13.9 1.0
CD A:GLN49 3.9 15.8 1.0
OE1 A:GLN49 4.2 17.2 1.0
CG A:HIS134 4.2 12.8 1.0
ND1 A:HIS134 4.2 13.9 1.0
ND1 A:HIS138 4.3 13.7 1.0
N A:LEU93 4.3 13.7 1.0
CG A:HIS138 4.3 12.7 1.0
C5 A:BB2154 4.3 15.9 1.0
C A:CYS92 4.5 14.5 1.0
OE1 A:GLU135 4.5 15.5 1.0
O A:HOH205 4.6 16.0 1.0
C6 A:BB2154 4.7 17.4 1.0
N A:SER94 4.9 13.6 1.0
CG A:GLN49 4.9 14.3 1.0
OE2 A:GLU135 4.9 14.6 1.0
C7 A:BB2154 5.0 18.1 1.0

Reference:

J.A.Frank, D.Lorimer, M.Youle, P.Witte, T.Craig, J.Abendroth, F.Rohwer, R.A.Edwards, A.M.Segall, A.B.Burgin. Structure and Function of A Cyanophage-Encoded Peptide Deformylase. Isme J V. 7 1150 2013.
ISSN: ISSN 1751-7362
PubMed: 23407310
DOI: 10.1038/ISMEJ.2013.4
Page generated: Sat Oct 26 17:29:54 2024

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