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Zinc in PDB 1mxg: Crystal Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose

Enzymatic activity of Crystal Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose

All present enzymatic activity of Crystal Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose:
3.2.1.1;

Protein crystallography data

The structure of Crystal Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose, PDB code: 1mxg was solved by A.Linden, O.Mayans, W.Meyer-Klaucke, G.Antranikian, M.Wilmanns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.480, 76.507, 136.455, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 17.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose (pdb code 1mxg). 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 Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose, PDB code: 1mxg:

Zinc binding site 1 out of 1 in 1mxg

Go back to Zinc Binding Sites List in 1mxg
Zinc binding site 1 out of 1 in the Crystal Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Strucutre of A (Ca,Zn)-Dependent Alpha-Amylase From the Hyperthermophilic Archaeon Pyrococcus Woesei in Complex with Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn437

b:12.7
occ:1.00
NE2 A:HIS152 2.0 15.8 1.0
NE2 A:HIS147 2.0 13.5 1.0
O A:HOH482 2.1 13.8 1.0
SG A:CYS166 2.3 12.6 1.0
CE1 A:HIS152 2.8 19.2 1.0
CD2 A:HIS147 2.9 11.8 1.0
CE1 A:HIS147 3.1 11.9 1.0
CD2 A:HIS152 3.1 19.3 1.0
CB A:CYS166 3.1 11.1 1.0
CA A:CYS166 3.4 10.6 1.0
ND1 A:HIS168 3.8 14.8 1.0
ND1 A:HIS152 4.0 20.3 1.0
CG A:HIS147 4.1 10.3 1.0
C A:CYS166 4.1 11.3 1.0
CG A:HIS152 4.2 18.9 1.0
ND1 A:HIS147 4.2 11.0 1.0
O A:HOH465 4.3 11.6 1.0
CB A:HIS168 4.4 12.7 1.0
N A:HIS167 4.4 10.0 1.0
CG A:HIS168 4.5 13.3 1.0
ND2 A:ASN149 4.5 13.4 1.0
N A:HIS168 4.5 11.6 1.0
N A:CYS166 4.7 11.0 1.0
CB A:ASP155 4.7 15.4 1.0
CE1 A:HIS168 4.8 14.8 1.0
O A:CYS166 4.9 10.5 1.0
O A:ILE165 5.0 10.6 1.0

Reference:

A.Linden, O.Mayans, W.Meyer-Klaucke, G.Antranikian, M.Wilmanns. Differential Regulation of A Hyperthermophilic Alpha-Amylase with A Novel (Ca,Zn) Two-Metal Center By Zinc J.Biol.Chem. V. 278 9875 2003.
ISSN: ISSN 0021-9258
PubMed: 12482867
DOI: 10.1074/JBC.M211339200
Page generated: Fri Sep 25 22:38:15 2020
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