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Zinc in PDB 1ekm: Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli

Enzymatic activity of Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli

All present enzymatic activity of Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli, PDB code: 1ekm was solved by Z.Chen, B.Schwartz, N.K.Williams, R.Li, J.P.Klinman, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 500.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 139.227, 153.515, 223.407, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 20.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli (pdb code 1ekm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli, PDB code: 1ekm:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 1ekm

Go back to Zinc Binding Sites List in 1ekm
Zinc binding site 1 out of 3 in the Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:21.4
occ:1.00
 ND1 A:HIS624 1.9 20.9 1.0
NE2 A:HIS456 2.0 14.0 1.0
OH A:TYR405 2.0 22.5 1.0
NE2 A:HIS458 2.1 15.1 1.0
CE1 A:HIS624 2.8 20.0 1.0
CE1 A:HIS456 2.9 14.8 1.0
CZ A:TYR405 2.9 22.5 1.0
CG A:HIS624 3.0 20.3 1.0
CD2 A:HIS458 3.1 15.2 1.0
CD2 A:HIS456 3.1 14.2 1.0
CE1 A:HIS458 3.1 15.2 1.0
CB A:HIS624 3.5 17.6 1.0
CE2 A:TYR405 3.6 22.5 1.0
CE1 A:TYR405 3.7 22.4 1.0
CD2 A:LEU425 3.8 26.2 1.0
O A:HOH702 3.8 21.6 1.0
NE2 A:HIS624 3.9 20.8 1.0
ND1 A:HIS456 4.1 15.1 1.0
CD2 A:HIS624 4.1 21.4 1.0
CG A:HIS456 4.2 15.1 1.0
ND1 A:HIS458 4.2 15.4 1.0
CG A:HIS458 4.3 14.9 1.0
CD2 A:LEU429 4.6 13.8 1.0
CD2 A:TYR405 4.8 22.8 1.0
CD1 A:TYR405 4.9 23.1 1.0
OH A:TYR305 4.9 18.5 1.0

Zinc binding site 2 out of 3 in 1ekm

Go back to Zinc Binding Sites List in 1ekm
Zinc binding site 2 out of 3 in the Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn701

b:21.4
occ:1.00
 ND1 B:HIS624 1.9 20.9 1.0
NE2 B:HIS456 2.0 14.0 1.0
OH B:TYR405 2.0 22.5 1.0
NE2 B:HIS458 2.1 15.1 1.0
CE1 B:HIS624 2.8 20.0 1.0
CE1 B:HIS456 2.9 14.8 1.0
CZ B:TYR405 2.9 22.5 1.0
CG B:HIS624 3.0 20.3 1.0
CD2 B:HIS458 3.1 15.2 1.0
CD2 B:HIS456 3.1 14.2 1.0
CE1 B:HIS458 3.1 15.2 1.0
CB B:HIS624 3.5 17.6 1.0
CE2 B:TYR405 3.6 22.5 1.0
CE1 B:TYR405 3.7 22.4 1.0
CD2 B:LEU425 3.8 26.2 1.0
O B:HOH809 3.8 21.6 1.0
NE2 B:HIS624 3.9 20.8 1.0
ND1 B:HIS456 4.1 15.1 1.0
CD2 B:HIS624 4.1 21.4 1.0
CG B:HIS456 4.2 15.1 1.0
ND1 B:HIS458 4.2 15.4 1.0
CG B:HIS458 4.3 14.9 1.0
CD2 B:LEU429 4.6 13.8 1.0
CD2 B:TYR405 4.8 22.8 1.0
CD1 B:TYR405 4.9 23.1 1.0
OH B:TYR305 4.9 18.5 1.0

Zinc binding site 3 out of 3 in 1ekm

Go back to Zinc Binding Sites List in 1ekm
Zinc binding site 3 out of 3 in the Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn701

b:21.4
occ:1.00
 ND1 C:HIS624 1.9 20.9 1.0
NE2 C:HIS456 2.0 14.0 1.0
OH C:TYR405 2.0 22.5 1.0
NE2 C:HIS458 2.1 15.1 1.0
CE1 C:HIS624 2.8 20.0 1.0
CE1 C:HIS456 2.9 14.8 1.0
CZ C:TYR405 2.9 22.5 1.0
CG C:HIS624 3.0 20.3 1.0
CD2 C:HIS458 3.1 15.2 1.0
CD2 C:HIS456 3.1 14.2 1.0
CE1 C:HIS458 3.1 15.2 1.0
CB C:HIS624 3.5 17.6 1.0
CE2 C:TYR405 3.6 22.5 1.0
CE1 C:TYR405 3.7 22.4 1.0
CD2 C:LEU425 3.8 26.2 1.0
O C:HOH719 3.8 21.6 1.0
NE2 C:HIS624 3.9 20.8 1.0
ND1 C:HIS456 4.1 15.1 1.0
CD2 C:HIS624 4.1 21.4 1.0
CG C:HIS456 4.2 15.1 1.0
ND1 C:HIS458 4.2 15.4 1.0
CG C:HIS458 4.3 14.9 1.0
CD2 C:LEU429 4.6 13.8 1.0
CD2 C:TYR405 4.8 22.8 1.0
CD1 C:TYR405 4.9 23.1 1.0
OH C:TYR305 4.9 18.5 1.0

Reference:

Z.Chen, B.Schwartz, N.K.Williams, R.Li, J.P.Klinman, F.S.Mathews. Crystal Structure at 2.5 A Resolution of Zinc-Substituted Copper Amine Oxidase of Hansenula Polymorpha Expressed in Escherichia Coli. Biochemistry V. 39 9709 2000.
ISSN: ISSN 0006-2960
PubMed: 10933787
DOI: 10.1021/BI000639F
Page generated: Sun Oct 13 00:14:42 2024

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