Atomistry » Zinc » PDB 1ed8-1evl » 1ekm
Atomistry »
  Zinc »
    PDB 1ed8-1evl »
      1ekm »

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

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy