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Zinc in PDB 4mtu: Beta-Alanyl-Coa:Ammonia Lyase From Clostridium Propionicum

Protein crystallography data

The structure of Beta-Alanyl-Coa:Ammonia Lyase From Clostridium Propionicum, PDB code: 4mtu was solved by A.Heine, K.Reuter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 0.97
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 78.110, 78.110, 102.810, 90.00, 90.00, 120.00
R / Rfree (%) 12.9 / 15.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Beta-Alanyl-Coa:Ammonia Lyase From Clostridium Propionicum (pdb code 4mtu). 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 Beta-Alanyl-Coa:Ammonia Lyase From Clostridium Propionicum, PDB code: 4mtu:

Zinc binding site 1 out of 1 in 4mtu

Go back to Zinc Binding Sites List in 4mtu
Zinc binding site 1 out of 1 in the Beta-Alanyl-Coa:Ammonia Lyase From Clostridium Propionicum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Beta-Alanyl-Coa:Ammonia Lyase From Clostridium Propionicum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:14.9
occ:1.00
NE2 A:HIS142 2.0 16.8 1.0
O A:HOH394 2.1 16.9 1.0
O A:HOH363 2.1 17.2 1.0
OD2 A:ASP45 2.1 13.9 1.0
O A:HOH387 2.2 16.1 1.0
OD1 A:ASP45 2.3 14.7 1.0
CG A:ASP45 2.6 12.7 1.0
CE1 A:HIS142 3.0 15.8 1.0
CD2 A:HIS142 3.0 18.3 1.0
OE1 A:GLN129 3.9 17.7 1.0
O A:HOH407 4.0 32.3 1.0
CB A:ASP45 4.1 12.2 1.0
O A:VAL44 4.1 13.2 1.0
ND1 A:HIS142 4.1 16.7 1.0
CG A:HIS142 4.2 17.6 1.0
CA A:GLY131 4.2 13.6 1.0
N A:GLY131 4.4 13.2 1.0
O A:ALA140 4.5 20.4 0.4
OH A:TYR83 4.6 16.0 1.0
CB A:GLN129 4.6 13.9 1.0
CD A:GLN129 4.8 15.7 1.0
CA A:ASP45 4.8 11.5 1.0
C A:GLY131 5.0 13.1 1.0
CD A:PRO132 5.0 15.4 1.0

Reference:

A.Heine, G.Herrmann, T.Selmer, F.Terwesten, W.Buckel, K.Reuter. High Resolution Crystal Structure of Clostridium Propionicum Beta-Alanyl-Coa:Ammonia Lyase, A New Member of the "Hot Dog Fold" Protein Superfamily. Proteins V. 82 2041 2014.
ISSN: ISSN 0887-3585
PubMed: 24623648
DOI: 10.1002/PROT.24557
Page generated: Wed Dec 16 05:36:00 2020

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