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Copper in PDB 4eis: Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3)

Protein crystallography data

The structure of Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3), PDB code: 4eis was solved by X.Li, W.T.Beeson, C.M.Phillips, M.A.Marletta, J.H.Cate, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.74 / 1.37
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 35.740, 77.890, 82.050, 90.00, 90.02, 90.00
R / Rfree (%) 11.6 / 14.9

Copper Binding Sites:

The binding sites of Copper atom in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3) (pdb code 4eis). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3), PDB code: 4eis:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 4eis

Go back to Copper Binding Sites List in 4eis
Copper binding site 1 out of 2 in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:13.0
occ:1.00
HE2 A:HIS82 1.3 10.5 1.0
ND1 A:HIC1 2.0 12.7 1.0
NE2 A:HIS82 2.1 12.0 1.0
N A:HIC1 2.3 13.5 1.0
H A:HIC1 2.6 11.9 1.0
OH A:TYR171 2.7 10.4 1.0
H2 A:HIC1 2.8 12.8 1.0
CD2 A:HIS82 2.9 11.4 1.0
CG A:HIC1 2.9 12.5 1.0
CE1 A:HIC1 3.0 13.4 1.0
HD2 A:HIS82 3.0 10.8 1.0
HH A:TYR171 3.0 10.6 1.0
CE1 A:HIS82 3.2 11.6 1.0
CA A:HIC1 3.2 11.2 1.0
HE1 A:HIC1 3.3 14.7 1.0
CB A:HIC1 3.3 11.3 1.0
HB3 A:HIC1 3.4 11.7 1.0
O1 A:PER302 3.4 38.5 1.0
HA A:HIC1 3.5 10.9 1.0
HE1 A:HIS82 3.5 11.9 1.0
O A:HOH401 3.6 29.8 1.0
CZ A:TYR171 3.8 10.3 1.0
OE1 A:GLN169 3.8 12.2 1.0
HG3 A:PRO79 4.0 11.1 1.0
HG2 A:PRO79 4.0 9.3 1.0
CG A:HIS82 4.1 9.8 1.0
CD2 A:HIC1 4.1 13.3 1.0
NE2 A:HIC1 4.1 15.4 1.0
ND1 A:HIS82 4.2 12.4 1.0
HE1 A:TYR171 4.2 9.6 1.0
HE1 A:HIS160 4.3 14.8 1.0
O2 A:PER302 4.3 38.2 1.0
HD3 A:PRO41 4.4 12.1 1.0
CE1 A:TYR171 4.4 9.5 1.0
HB2 A:HIC1 4.4 11.4 1.0
CG A:PRO79 4.4 11.8 1.0
C A:HIC1 4.5 9.8 1.0
HE2 A:HIS160 4.6 15.8 1.0
HE2 A:TYR171 4.6 9.2 1.0
CE2 A:TYR171 4.6 9.5 1.0
HE1 B:TYR24 4.7 17.1 1.0
O A:HOH562 4.8 32.5 1.0
O A:HOH616 4.9 45.1 1.0
CD A:GLN169 5.0 12.0 1.0
O A:HIC1 5.0 12.1 1.0
CE1 A:HIS160 5.0 15.4 1.0

Copper binding site 2 out of 2 in 4eis

Go back to Copper Binding Sites List in 4eis
Copper binding site 2 out of 2 in the Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases (Pmo-3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu301

b:12.0
occ:1.00
HE2 B:HIS82 1.2 10.5 1.0
ND1 B:HIC1 1.9 12.2 1.0
NE2 B:HIS82 2.1 10.3 1.0
N B:HIC1 2.3 10.3 1.0
O B:HOH401 2.3 25.5 0.9
H2 B:HIC1 2.6 10.8 1.0
CG B:HIC1 2.8 8.5 1.0
OH B:TYR171 2.8 11.7 1.0
H B:HIC1 2.9 10.5 1.0
CE1 B:HIC1 3.0 11.6 1.0
CD2 B:HIS82 3.0 11.1 1.0
CE1 B:HIS82 3.1 11.7 1.0
CA B:HIC1 3.1 10.1 1.0
HD2 B:HIS82 3.2 11.1 1.0
HH B:TYR171 3.2 10.6 1.0
HB3 B:HIC1 3.2 9.8 1.0
CB B:HIC1 3.2 8.9 1.0
HE1 B:HIC1 3.3 12.0 1.0
HA B:HIC1 3.3 9.6 1.0
HE1 B:HIS82 3.4 12.5 1.0
HG2 B:PRO79 3.6 10.8 1.0
CZ B:TYR171 3.8 9.9 1.0
OE1 B:GLN169 3.9 12.6 1.0
CD2 B:HIC1 4.0 9.4 1.0
HE1 B:TYR171 4.0 9.3 1.0
NE2 B:HIC1 4.0 11.1 1.0
CG B:HIS82 4.1 10.1 1.0
ND1 B:HIS82 4.1 11.4 1.0
HD3 B:PRO41 4.2 9.3 1.0
HB2 B:HIC1 4.3 8.7 1.0
HB2 A:DAH24 4.3 16.4 1.0
CE1 B:TYR171 4.3 9.9 1.0
C B:HIC1 4.4 9.5 1.0
HE1 B:HIS160 4.5 12.7 1.0
O B:HOH768 4.5 39.2 1.0
CG B:PRO79 4.5 11.1 1.0
HE2 B:HIS160 4.6 13.1 1.0
CE2 B:TYR171 4.8 8.7 1.0
HG3 B:PRO79 4.8 10.6 1.0
O B:HIC1 4.9 9.6 1.0
HE2 B:TYR171 4.9 8.4 1.0
HD2 A:DAH24 4.9 18.1 1.0
CD2 A:DAH24 4.9 19.1 1.0
HD2 B:HIC1 5.0 9.6 1.0

Reference:

X.Li, W.T.Beeson, C.M.Phillips, M.A.Marletta, J.H.Cate. Structural Basis For Substrate Targeting and Catalysis By Fungal Polysaccharide Monooxygenases. Structure V. 20 1051 2012.
ISSN: ISSN 0969-2126
PubMed: 22578542
DOI: 10.1016/J.STR.2012.04.002
Page generated: Mon Jul 14 03:37:35 2025

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