Copper in PDB 6vox: Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva
Protein crystallography data
The structure of Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva, PDB code: 6vox
was solved by
S.H.Partowmah,
E.A.Coler,
A.S.Soares,
R.E.Collins,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
3.80
|
Space group
|
P 62 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
170.35,
170.35,
131,
90,
90,
120
|
R / Rfree (%)
|
25.8 /
27.4
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva
(pdb code 6vox). 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 Multi-Copper Oxidase From Pseudomonas Parafulva, PDB code: 6vox:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 6vox
Go back to
Copper Binding Sites List in 6vox
Copper binding site 1 out
of 4 in the Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva
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 Multi-Copper Oxidase From Pseudomonas Parafulva within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:85.0
occ:0.80
|
CU2
|
A:C2O501
|
0.0
|
85.0
|
0.8
|
O1
|
A:C2O501
|
2.3
|
82.3
|
0.8
|
ND1
|
A:HIS98
|
2.3
|
130.9
|
1.0
|
NE2
|
A:HIS444
|
2.6
|
169.8
|
1.0
|
NE2
|
A:HIS138
|
2.7
|
147.5
|
1.0
|
CE1
|
A:HIS138
|
2.8
|
148.3
|
1.0
|
CE1
|
A:HIS98
|
2.9
|
154.6
|
1.0
|
CD2
|
A:HIS444
|
3.1
|
173.4
|
1.0
|
CE1
|
A:HIS444
|
3.3
|
165.3
|
1.0
|
CG
|
A:HIS98
|
3.4
|
127.5
|
1.0
|
NE2
|
A:HIS96
|
3.5
|
184.7
|
1.0
|
CD2
|
A:HIS96
|
3.5
|
182.3
|
1.0
|
CD2
|
A:HIS394
|
3.6
|
139.3
|
1.0
|
CU3
|
A:C2O501
|
3.7
|
93.5
|
0.8
|
CZ2
|
A:TRP136
|
3.8
|
96.0
|
1.0
|
NE2
|
A:HIS394
|
3.8
|
143.7
|
1.0
|
CB
|
A:HIS98
|
3.9
|
123.8
|
1.0
|
CU
|
A:CU502
|
4.0
|
109.3
|
0.8
|
CD2
|
A:HIS138
|
4.0
|
154.8
|
1.0
|
ND1
|
A:HIS138
|
4.1
|
148.4
|
1.0
|
CG
|
A:HIS444
|
4.1
|
155.3
|
1.0
|
NE2
|
A:HIS98
|
4.1
|
162.2
|
1.0
|
ND1
|
A:HIS444
|
4.2
|
165.7
|
1.0
|
CD2
|
A:HIS98
|
4.3
|
145.6
|
1.0
|
CH2
|
A:TRP136
|
4.4
|
108.2
|
1.0
|
CE2
|
A:TRP136
|
4.5
|
112.7
|
1.0
|
CE1
|
A:HIS96
|
4.5
|
185.9
|
1.0
|
CG
|
A:HIS394
|
4.6
|
154.0
|
1.0
|
CG
|
A:HIS96
|
4.6
|
169.3
|
1.0
|
NE2
|
A:HIS140
|
4.6
|
178.1
|
1.0
|
CG
|
A:HIS138
|
4.7
|
145.7
|
1.0
|
CA
|
A:HIS98
|
4.7
|
148.2
|
1.0
|
CD2
|
A:HIS140
|
4.8
|
194.4
|
1.0
|
NE1
|
A:TRP136
|
4.8
|
130.0
|
1.0
|
CE1
|
A:HIS394
|
4.8
|
158.3
|
1.0
|
|
Copper binding site 2 out
of 4 in 6vox
Go back to
Copper Binding Sites List in 6vox
Copper binding site 2 out
of 4 in the Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva
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 Multi-Copper Oxidase From Pseudomonas Parafulva within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:93.5
occ:0.80
|
CU3
|
A:C2O501
|
0.0
|
93.5
|
0.8
|
O1
|
A:C2O501
|
1.8
|
82.3
|
0.8
|
NE2
|
A:HIS96
|
2.2
|
184.7
|
1.0
|
NE2
|
A:HIS140
|
2.6
|
178.1
|
1.0
|
NE2
|
A:HIS396
|
2.7
|
140.0
|
1.0
|
CD2
|
A:HIS96
|
2.7
|
182.3
|
1.0
|
CE1
|
A:HIS396
|
2.9
|
167.6
|
1.0
|
CD2
|
A:HIS140
|
3.0
|
194.4
|
1.0
|
NE2
|
A:HIS442
|
3.1
|
146.4
|
1.0
|
CE1
|
A:HIS96
|
3.3
|
185.9
|
1.0
|
CE1
|
A:HIS140
|
3.4
|
188.0
|
1.0
|
NE2
|
A:HIS394
|
3.5
|
143.7
|
1.0
|
CD2
|
A:HIS396
|
3.5
|
156.3
|
1.0
|
CD2
|
A:HIS394
|
3.6
|
139.3
|
1.0
|
CU
|
A:CU502
|
3.6
|
109.3
|
0.8
|
CU2
|
A:C2O501
|
3.7
|
85.0
|
0.8
|
ND1
|
A:HIS396
|
3.8
|
193.1
|
1.0
|
CD2
|
A:HIS442
|
3.9
|
152.4
|
1.0
|
CG
|
A:HIS140
|
3.9
|
198.5
|
1.0
|
CG
|
A:HIS96
|
3.9
|
169.3
|
1.0
|
ND1
|
A:HIS140
|
4.1
|
198.4
|
1.0
|
CE1
|
A:HIS442
|
4.1
|
187.8
|
1.0
|
CG
|
A:HIS396
|
4.1
|
176.9
|
1.0
|
ND1
|
A:HIS96
|
4.2
|
173.4
|
1.0
|
CE1
|
A:HIS394
|
4.8
|
158.3
|
1.0
|
CE1
|
A:HIS138
|
4.8
|
148.3
|
1.0
|
ND1
|
A:HIS98
|
4.9
|
130.9
|
1.0
|
CD2
|
A:HIS444
|
4.9
|
173.4
|
1.0
|
CG
|
A:HIS394
|
4.9
|
154.0
|
1.0
|
|
Copper binding site 3 out
of 4 in 6vox
Go back to
Copper Binding Sites List in 6vox
Copper binding site 3 out
of 4 in the Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva
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 Multi-Copper Oxidase From Pseudomonas Parafulva within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:109.3
occ:0.80
|
CE1
|
A:HIS96
|
2.1
|
185.9
|
1.0
|
NE2
|
A:HIS96
|
2.3
|
184.7
|
1.0
|
NE2
|
A:HIS394
|
2.3
|
143.7
|
1.0
|
CE1
|
A:HIS394
|
2.8
|
158.3
|
1.0
|
ND1
|
A:HIS98
|
3.2
|
130.9
|
1.0
|
CA
|
A:HIS98
|
3.2
|
148.2
|
1.0
|
N
|
A:GLY99
|
3.2
|
183.7
|
1.0
|
ND1
|
A:HIS96
|
3.3
|
173.4
|
1.0
|
CD2
|
A:HIS96
|
3.5
|
182.3
|
1.0
|
CD2
|
A:HIS394
|
3.5
|
139.3
|
1.0
|
CG
|
A:HIS396
|
3.6
|
176.9
|
1.0
|
CU3
|
A:C2O501
|
3.6
|
93.5
|
0.8
|
CG
|
A:HIS98
|
3.7
|
127.5
|
1.0
|
CD2
|
A:HIS396
|
3.7
|
156.3
|
1.0
|
C
|
A:HIS98
|
3.7
|
166.1
|
1.0
|
O1
|
A:C2O501
|
3.8
|
82.3
|
0.8
|
CB
|
A:HIS98
|
3.8
|
123.8
|
1.0
|
O
|
A:TRP97
|
3.9
|
124.5
|
1.0
|
CB
|
A:HIS396
|
3.9
|
164.2
|
1.0
|
CE1
|
A:HIS98
|
3.9
|
154.6
|
1.0
|
CG
|
A:HIS96
|
4.0
|
169.3
|
1.0
|
CU2
|
A:C2O501
|
4.0
|
85.0
|
0.8
|
ND1
|
A:HIS396
|
4.0
|
193.1
|
1.0
|
ND1
|
A:HIS394
|
4.1
|
162.6
|
1.0
|
CA
|
A:HIS396
|
4.1
|
139.7
|
1.0
|
N
|
A:HIS98
|
4.1
|
155.4
|
1.0
|
NE2
|
A:HIS396
|
4.2
|
140.0
|
1.0
|
C
|
A:LEU395
|
4.2
|
153.7
|
1.0
|
CA
|
A:GLY99
|
4.2
|
165.7
|
1.0
|
N
|
A:HIS396
|
4.3
|
133.2
|
1.0
|
C
|
A:TRP97
|
4.3
|
154.8
|
1.0
|
CE1
|
A:HIS396
|
4.4
|
167.6
|
1.0
|
CG
|
A:HIS394
|
4.4
|
154.0
|
1.0
|
O
|
A:LEU395
|
4.5
|
148.8
|
1.0
|
CD2
|
A:HIS98
|
4.6
|
145.6
|
1.0
|
NE2
|
A:HIS98
|
4.7
|
162.2
|
1.0
|
C
|
A:GLY99
|
4.7
|
160.2
|
1.0
|
O
|
A:GLY99
|
4.8
|
153.2
|
1.0
|
OD2
|
A:ASP107
|
4.9
|
200.6
|
1.0
|
O
|
A:HIS98
|
4.9
|
143.6
|
1.0
|
|
Copper binding site 4 out
of 4 in 6vox
Go back to
Copper Binding Sites List in 6vox
Copper binding site 4 out
of 4 in the Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva
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 Multi-Copper Oxidase From Pseudomonas Parafulva within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:113.5
occ:0.80
|
SG
|
A:CYS443
|
2.2
|
98.9
|
1.0
|
ND1
|
A:HIS391
|
2.4
|
112.8
|
1.0
|
ND1
|
A:HIS448
|
2.5
|
118.9
|
1.0
|
CG
|
A:HIS391
|
2.9
|
118.9
|
1.0
|
CB
|
A:VAL445
|
3.1
|
152.8
|
1.0
|
CE1
|
A:HIS391
|
3.1
|
110.9
|
1.0
|
CG
|
A:HIS448
|
3.2
|
129.8
|
1.0
|
CG2
|
A:VAL445
|
3.3
|
151.6
|
1.0
|
CB
|
A:HIS391
|
3.4
|
120.4
|
1.0
|
CE1
|
A:HIS448
|
3.4
|
123.2
|
1.0
|
CB
|
A:HIS448
|
3.4
|
153.0
|
1.0
|
CA
|
A:HIS391
|
3.5
|
129.3
|
1.0
|
CG1
|
A:VAL445
|
3.8
|
156.1
|
1.0
|
CB
|
A:CYS443
|
3.8
|
109.0
|
1.0
|
CD2
|
A:HIS391
|
3.8
|
117.8
|
1.0
|
CD
|
A:PRO392
|
3.8
|
143.3
|
1.0
|
NE2
|
A:HIS391
|
3.8
|
119.8
|
1.0
|
O
|
A:GLN390
|
4.0
|
167.2
|
1.0
|
CD2
|
A:HIS448
|
4.3
|
120.7
|
1.0
|
CA
|
A:VAL445
|
4.3
|
146.9
|
1.0
|
NE2
|
A:HIS448
|
4.3
|
126.1
|
1.0
|
N
|
A:VAL445
|
4.4
|
138.5
|
1.0
|
N
|
A:HIS391
|
4.5
|
133.8
|
1.0
|
N
|
A:PRO392
|
4.5
|
147.8
|
1.0
|
C
|
A:HIS391
|
4.5
|
138.5
|
1.0
|
C
|
A:GLN390
|
4.5
|
148.3
|
1.0
|
O
|
A:VAL445
|
4.8
|
133.6
|
1.0
|
CA
|
A:CYS443
|
4.9
|
119.2
|
1.0
|
CD2
|
A:LEU453
|
4.9
|
144.0
|
1.0
|
C
|
A:CYS443
|
4.9
|
125.4
|
1.0
|
CA
|
A:HIS448
|
4.9
|
167.2
|
1.0
|
O
|
A:ASN196
|
5.0
|
148.4
|
1.0
|
CG
|
A:PRO392
|
5.0
|
139.5
|
1.0
|
O
|
A:CYS443
|
5.0
|
122.9
|
1.0
|
|
Reference:
S.Partowmah,
E.A.Coler,
A.S.Soares,
R.E.Collins.
Crystal Structure of Multi-Copper Oxidase From Pseudomonas Parafulva To Be Published.
Page generated: Wed Jul 31 07:42:59 2024
|