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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

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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

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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

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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

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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: Thu Sep 3 15:57:41 2020
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