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Zinc in PDB 1jwq: Structure of the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus

Enzymatic activity of Structure of the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus

All present enzymatic activity of Structure of the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus:
3.5.1.28;

Protein crystallography data

The structure of Structure of the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus, PDB code: 1jwq was solved by T.Yamane, Y.Koyama, Y.Nojiri, T.Hikage, M.Akita, A.Suzuki, T.Shirai, F.Ise, T.Shida, J.Sekiguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 66.500, 66.500, 88.340, 90.00, 90.00, 120.00
R / Rfree (%) 17.6 / 20.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus (pdb code 1jwq). 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 the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus, PDB code: 1jwq:

Zinc binding site 1 out of 1 in 1jwq

Go back to Zinc Binding Sites List in 1jwq
Zinc binding site 1 out of 1 in the Structure of the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Catalytic Domain of Cwlv, N-Acetylmuramoyl- L-Alanine Amidase From Bacillus(Paenibacillus) Polymyxa Var.Colistinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:16.9
occ:1.00
O A:HOH1048 2.0 13.1 1.0
OE1 A:GLU26 2.0 11.3 1.0
NE2 A:HIS10 2.1 10.1 1.0
ND1 A:HIS80 2.2 9.4 1.0
O A:HOH1047 2.3 15.6 1.0
CD A:GLU26 2.8 12.3 1.0
OE2 A:GLU26 3.0 11.8 1.0
O A:HOH1052 3.0 25.4 1.0
CD2 A:HIS10 3.1 10.9 1.0
CE1 A:HIS80 3.1 10.1 1.0
CE1 A:HIS10 3.1 11.8 1.0
CG A:HIS80 3.2 9.5 1.0
CB A:HIS80 3.5 8.4 1.0
O A:ALA81 4.0 14.0 1.0
OE1 A:GLU142 4.2 18.9 1.0
CG A:HIS10 4.2 11.1 1.0
ND1 A:HIS10 4.2 11.4 1.0
NE2 A:HIS80 4.2 8.8 1.0
CG A:GLU26 4.3 12.2 1.0
CD2 A:HIS80 4.3 6.2 1.0
CA A:HIS80 4.4 9.4 1.0
O A:HOH1075 4.5 21.1 1.0
N A:ALA81 4.5 11.3 1.0
ND2 A:ASN30 4.5 9.4 1.0
O A:HOH1019 4.8 16.2 1.0
O A:HOH1117 4.9 32.7 1.0
OE2 A:GLU142 4.9 18.1 1.0
CD A:GLU142 5.0 17.2 1.0

Reference:

T.Yamane, Y.Koyama, Y.Nojiri, T.Hikage, M.Akita, A.Suzuki, T.Shirai, F.Ise, T.Shida, J.Sekiguchi. The Structure of the Catalytic Domain of N-Acetylmuramoyl-L-Alanine Amidase, A Cell Wall Hydrolase From Bacillus Polymyxa Var.Colistinus and Its Resemblance to the Structure of Carboxypeptidases To Be Published.
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