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Zinc in PDB 4cwd: Crystal Structure of Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate

Enzymatic activity of Crystal Structure of Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate

All present enzymatic activity of Crystal Structure of Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate:
1.14.11.1;

Protein crystallography data

The structure of Crystal Structure of Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate, PDB code: 4cwd was solved by M.A.Mcdonough, G.Kochan, A.Rydzik, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.826 / 1.90
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 106.518, 106.518, 205.347, 90.00, 90.00, 120.00
R / Rfree (%) 16.74 / 20.62

Other elements in 4cwd:

The structure of Crystal Structure of Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate also contains other interesting chemical elements:

Nickel (Ni) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate (pdb code 4cwd). 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 Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate, PDB code: 4cwd:

Zinc binding site 1 out of 1 in 4cwd

Go back to Zinc Binding Sites List in 4cwd
Zinc binding site 1 out of 1 in the Crystal Structure of Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate


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 Human Gamma-Butyrobetaine,2- Oxoglutarate in Complex with 449, A Novel Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn389

b:18.2
occ:1.00
 NE2 A:HIS82 2.1 18.9 1.0
SG A:CYS38 2.2 19.9 1.0
SG A:CYS43 2.3 17.1 1.0
SG A:CYS40 2.4 21.9 1.0
CE1 A:HIS82 3.0 20.1 1.0
CD2 A:HIS82 3.2 18.4 1.0
CB A:CYS38 3.2 19.4 1.0
CB A:CYS43 3.3 20.5 1.0
CB A:CYS40 3.4 22.9 1.0
NH1 A:ARG35 4.0 15.9 1.0
N A:CYS40 4.1 19.2 1.0
ND1 A:HIS82 4.1 18.2 1.0
N A:CYS43 4.2 18.2 1.0
CA A:CYS40 4.2 21.5 1.0
CG A:HIS82 4.3 19.9 1.0
O A:HOH2058 4.3 36.6 1.0
O A:TYR83 4.3 20.2 1.0
CA A:CYS43 4.4 19.2 1.0
O A:HOH2043 4.4 26.6 1.0
CA A:CYS38 4.5 17.9 1.0
OG A:SER84 4.5 18.8 1.0
C A:CYS38 4.5 17.1 1.0
O A:CYS38 4.5 18.5 1.0
O A:CYS40 4.6 20.0 1.0
C A:CYS40 4.6 21.0 1.0
CZ A:ARG35 4.7 15.9 1.0
CB A:ASP42 4.8 22.7 1.0
NH2 A:ARG35 4.8 16.0 1.0

Reference:

A.M.Rydzik, I.K.H.Leung, G.T.Kochan, M.A.Mcdonough, T.D.W.Claridge, C.J.Schofield. Oxygenase-Catalyzed Desymmetrization of N,N-Dialkyl- Piperidine-4-Carboxylic Acids. Angew.Chem.Int.Ed.Engl. V. 53 10925 2014.
ISSN: ISSN 1433-7851
PubMed: 25164544
DOI: 10.1002/ANIE.201406125
Page generated: Sat Oct 26 21:07:30 2024

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