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Calcium in PDB 1mwo: Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase

Enzymatic activity of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase

All present enzymatic activity of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase:
3.2.1.1;

Protein crystallography data

The structure of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase, PDB code: 1mwo 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 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.880, 78.200, 106.289, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 22.4

Other elements in 1mwo:

The structure of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase (pdb code 1mwo). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase, PDB code: 1mwo:

Calcium binding site 1 out of 1 in 1mwo

Go back to Calcium Binding Sites List in 1mwo
Calcium binding site 1 out of 1 in the Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca442

b:27.1
occ:1.00
 OD1 A:ASP164 2.3 27.3 1.0
O A:GLY157 2.3 25.0 1.0
O A:GLY202 2.3 21.2 1.0
OD2 A:ASP155 2.3 22.9 1.0
O A:HOH478 2.5 19.7 1.0
ND2 A:ASN110 2.6 15.7 1.0
OD2 A:ASP164 2.6 26.6 1.0
OD1 A:ASP155 2.6 21.0 1.0
CG A:ASP164 2.8 25.0 1.0
CG A:ASP155 2.8 22.7 1.0
C A:GLY202 3.4 22.7 1.0
C A:GLY157 3.5 26.2 1.0
CG A:ASN110 3.6 19.6 1.0
N A:GLY157 4.0 26.1 1.0
CA A:GLY202 4.0 22.2 1.0
OD1 A:ASN110 4.0 20.3 1.0
O A:ASN110 4.2 21.9 1.0
CB A:ASP164 4.3 25.6 1.0
O A:HOH469 4.3 19.2 1.0
CA A:GLY157 4.3 25.4 1.0
CB A:ASP155 4.3 24.4 1.0
N A:THR158 4.5 26.9 1.0
N A:TYR203 4.5 22.1 1.0
CA A:THR158 4.6 29.2 1.0
O A:ILE165 4.6 22.8 1.0
ND1 A:HIS147 4.6 24.0 1.0
CE1 A:HIS147 4.6 24.8 1.0
O A:HOH500 4.7 18.4 1.0
CB A:TYR203 4.7 22.6 1.0
CA A:TYR203 4.8 23.0 1.0
CB A:ASN110 4.8 20.2 1.0
C A:ASN110 5.0 22.1 1.0
CA A:ASP164 5.0 23.7 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: Thu Jul 11 12:38:10 2024

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