Atomistry » Copper » PDB 1eso-1haw » 1h1i
Atomistry »
  Copper »
    PDB 1eso-1haw »
      1h1i »

Copper in PDB 1h1i: Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn

Enzymatic activity of Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn

All present enzymatic activity of Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn:
1.13.11.24;

Protein crystallography data

The structure of Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn, PDB code: 1h1i was solved by R.A.Steiner, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.39 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 109.298, 55.745, 124.163, 90.00, 98.39, 90.00
R / Rfree (%) 14.8 / 18.3

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn (pdb code 1h1i). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn, PDB code: 1h1i:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1h1i

Go back to Copper Binding Sites List in 1h1i
Copper binding site 1 out of 4 in the Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1357

b:19.6
occ:0.70
NE2 A:HIS112 2.1 14.4 1.0
O27 A:QUE1358 2.1 24.6 1.0
NE2 A:HIS68 2.1 13.6 1.0
NE2 A:HIS66 2.1 12.2 1.0
OE1 A:GLU73 2.3 27.4 1.0
CE1 A:HIS112 2.8 13.1 1.0
CE1 A:HIS68 2.9 13.1 1.0
C10 A:QUE1358 3.0 24.8 1.0
CE1 A:HIS66 3.1 13.7 1.0
CD A:GLU73 3.1 28.5 1.0
CD2 A:HIS66 3.1 11.3 1.0
CD2 A:HIS68 3.1 15.1 1.0
CD2 A:HIS112 3.2 11.7 1.0
O13 A:QUE1358 3.3 25.5 1.0
OE2 A:GLU73 3.4 32.2 1.0
C9 A:QUE1358 3.5 23.4 1.0
ND1 A:HIS112 4.0 10.2 1.0
ND1 A:HIS68 4.0 11.6 1.0
C11 A:QUE1358 4.0 21.5 1.0
CG A:HIS68 4.1 10.9 1.0
ND1 A:HIS66 4.2 12.7 1.0
CG A:HIS66 4.2 9.9 1.0
CG A:HIS112 4.2 9.8 1.0
CG A:GLU73 4.3 18.7 1.0
C19 A:QUE1358 4.4 23.2 1.0
C14 A:QUE1358 4.7 23.1 1.0
C3 A:QUE1358 4.9 20.5 1.0
CZ A:PHE75 4.9 13.4 1.0
CB A:GLU73 5.0 12.0 1.0

Copper binding site 2 out of 4 in 1h1i

Go back to Copper Binding Sites List in 1h1i
Copper binding site 2 out of 4 in the Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1355

b:17.6
occ:0.70
NE2 B:HIS112 2.0 11.5 1.0
NE2 B:HIS66 2.1 9.8 1.0
NE2 B:HIS68 2.1 13.1 1.0
OE1 B:GLU73 2.3 28.9 1.0
O27 B:QUE1356 2.3 25.6 1.0
CE1 B:HIS112 2.8 10.1 1.0
CE1 B:HIS68 2.9 12.3 1.0
CD2 B:HIS66 2.9 8.6 1.0
CE1 B:HIS66 3.1 10.4 1.0
CD2 B:HIS112 3.1 11.5 1.0
C10 B:QUE1356 3.2 23.1 1.0
CD2 B:HIS68 3.2 14.3 1.0
CD B:GLU73 3.3 27.5 1.0
O13 B:QUE1356 3.5 20.9 1.0
OE2 B:GLU73 3.6 31.0 1.0
C9 B:QUE1356 3.7 21.3 1.0
ND1 B:HIS112 3.9 10.2 1.0
ND1 B:HIS68 4.0 11.5 1.0
CG B:HIS66 4.1 9.8 1.0
ND1 B:HIS66 4.1 12.3 1.0
CG B:HIS112 4.1 10.1 1.0
C11 B:QUE1356 4.1 21.6 1.0
CG B:HIS68 4.2 11.4 1.0
C19 B:QUE1356 4.4 24.2 1.0
CG B:GLU73 4.6 19.5 1.0
C14 B:QUE1356 4.7 23.9 1.0
CZ B:PHE75 4.9 14.7 1.0

Copper binding site 3 out of 4 in 1h1i

Go back to Copper Binding Sites List in 1h1i
Copper binding site 3 out of 4 in the Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1357

b:17.0
occ:0.70
NE2 C:HIS112 2.0 9.1 1.0
NE2 C:HIS68 2.1 11.7 1.0
NE2 C:HIS66 2.1 12.1 1.0
O27 C:QUE1358 2.2 20.4 1.0
OE1 C:GLU73 2.3 28.7 1.0
CE1 C:HIS112 2.8 9.7 1.0
CD2 C:HIS68 3.0 10.8 1.0
CE1 C:HIS68 3.1 12.8 1.0
CD2 C:HIS66 3.1 10.4 1.0
CE1 C:HIS66 3.1 10.0 1.0
CD2 C:HIS112 3.1 11.2 1.0
CD C:GLU73 3.1 26.6 1.0
C10 C:QUE1358 3.2 18.2 1.0
OE2 C:GLU73 3.3 29.3 1.0
O13 C:QUE1358 3.5 20.1 1.0
C9 C:QUE1358 3.7 19.7 1.0
ND1 C:HIS112 4.0 9.1 1.0
ND1 C:HIS68 4.1 12.5 1.0
CG C:HIS68 4.1 9.3 1.0
CG C:HIS112 4.1 7.1 1.0
ND1 C:HIS66 4.2 10.3 1.0
C11 C:QUE1358 4.2 17.2 1.0
CG C:HIS66 4.2 7.1 1.0
C19 C:QUE1358 4.4 20.4 1.0
CG C:GLU73 4.5 21.0 1.0
C14 C:QUE1358 4.7 18.4 1.0
CZ C:PHE75 4.8 13.0 1.0

Copper binding site 4 out of 4 in 1h1i

Go back to Copper Binding Sites List in 1h1i
Copper binding site 4 out of 4 in the Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Quercetin 2,3-Dioxygenase Anaerobically Complexed with the Substrate Quercetn within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu1356

b:18.6
occ:0.70
NE2 D:HIS112 2.0 12.3 1.0
NE2 D:HIS66 2.1 13.4 1.0
O27 D:QUE1357 2.2 23.6 1.0
NE2 D:HIS68 2.2 16.5 1.0
OE1 D:GLU73 2.5 25.7 1.0
CE1 D:HIS112 2.8 9.9 1.0
CE1 D:HIS66 3.0 15.0 1.0
CD2 D:HIS66 3.0 9.9 1.0
CE1 D:HIS68 3.1 15.8 1.0
C10 D:QUE1357 3.1 22.4 1.0
CD D:GLU73 3.1 26.6 1.0
CD2 D:HIS68 3.1 16.0 1.0
CD2 D:HIS112 3.2 8.4 1.0
OE2 D:GLU73 3.4 31.0 1.0
O13 D:QUE1357 3.4 22.9 1.0
C9 D:QUE1357 3.6 22.6 1.0
ND1 D:HIS112 3.9 7.9 1.0
ND1 D:HIS66 4.1 13.2 1.0
ND1 D:HIS68 4.1 11.6 1.0
C11 D:QUE1357 4.1 20.1 1.0
CG D:HIS66 4.1 12.4 1.0
CG D:HIS112 4.2 7.9 1.0
CG D:HIS68 4.2 12.6 1.0
CG D:GLU73 4.3 18.6 1.0
C19 D:QUE1357 4.4 22.6 1.0
C14 D:QUE1357 4.7 22.1 1.0
C3 D:QUE1357 5.0 20.2 1.0

Reference:

R.A.Steiner, K.H.Kalk, B.W.Dijkstra. Anaerobic Enzyme.Substrate Structures Provide Insight Into the Reaction Mechanism of the Copper- Dependent Quercetin 2,3-Dioxygenase. Proc.Natl.Acad.Sci.Usa V. 99 16625 2002.
ISSN: ISSN 0027-8424
PubMed: 12486225
DOI: 10.1073/PNAS.262506299
Page generated: Sun Dec 13 10:59:09 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy