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: Wed Jul 31 02:50:13 2024
|