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Zinc in PDB 6nds: Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate

Enzymatic activity of Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate

All present enzymatic activity of Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate:
4.1.3.4;

Protein crystallography data

The structure of Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate, PDB code: 6nds was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.73 / 1.65
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.460, 91.460, 78.850, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 16.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate (pdb code 6nds). 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 Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate, PDB code: 6nds:

Zinc binding site 1 out of 1 in 6nds

Go back to Zinc Binding Sites List in 6nds
Zinc binding site 1 out of 1 in the Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn507

b:25.7
occ:1.00
 OD2 A:ASP17 2.1 21.8 1.0
O7 A:CIT502 2.1 25.7 1.0
O6 A:CIT502 2.2 25.8 1.0
NE2 A:HIS207 2.2 21.2 1.0
NE2 A:HIS209 2.2 24.5 1.0
O A:HOH623 2.2 25.4 1.0
C6 A:CIT502 2.9 27.8 1.0
C3 A:CIT502 3.0 34.9 1.0
CE1 A:HIS209 3.1 25.5 1.0
CG A:ASP17 3.1 26.0 1.0
CE1 A:HIS207 3.1 22.5 1.0
CD2 A:HIS207 3.2 19.1 1.0
CD2 A:HIS209 3.3 21.5 1.0
OD1 A:ASP17 3.4 27.3 1.0
C2 A:CIT502 3.9 33.4 1.0
ND2 A:ASN249 3.9 19.9 1.0
O4 A:CIT502 4.0 41.3 1.0
C4 A:CIT502 4.1 40.1 1.0
O5 A:CIT502 4.1 27.9 1.0
NH2 A:ARG16 4.1 28.4 1.0
C5 A:CIT502 4.2 51.8 1.0
ND1 A:HIS207 4.2 18.6 1.0
ND1 A:HIS209 4.2 21.9 1.0
O A:HOH718 4.2 28.1 1.0
CG A:HIS207 4.3 18.8 1.0
CG A:HIS209 4.4 23.2 1.0
CB A:ASP17 4.4 22.0 1.0
CG A:ASN249 4.7 21.2 1.0
NH1 A:ARG16 4.7 25.8 1.0
OD1 A:ASN249 4.7 24.0 1.0
CZ A:ARG16 4.9 24.6 1.0
O3 A:CIT502 5.0 55.1 1.0

Reference:

S.J.Mayclin, J.Abendroth, P.S.Horanyi, D.D.Lorimer, T.E.Edwards. Structure of An Hmg-Coa Lyase From Acenitobacter Baumannii in Complex with Coenzyme A and 3-Methylmalate To Be Published.
Page generated: Tue Oct 29 03:40:49 2024

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