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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

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