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Copper in PDB 1pf3: Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo

Protein crystallography data

The structure of Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo, PDB code: 1pf3 was solved by S.A.Roberts, G.F.Wildner, G.Grass, A.Weichsel, A.Ambrus, C.Rensing, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.445, 91.193, 53.905, 90.00, 102.35, 90.00
R / Rfree (%) 19.1 / 22.8

Other elements in 1pf3:

The structure of Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo (pdb code 1pf3). 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 the M441L Mutant of the Multicopper Oxidase Cueo, PDB code: 1pf3:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1pf3

Go back to Copper Binding Sites List in 1pf3
Copper binding site 1 out of 4 in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo


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 the M441L Mutant of the Multicopper Oxidase Cueo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:12.6
occ:0.50
ND1 A:HIS443 2.2 16.9 1.0
SG A:CYS500 2.2 16.4 1.0
ND1 A:HIS505 2.2 14.0 1.0
CE1 A:HIS443 3.1 20.0 1.0
CG A:HIS443 3.2 16.3 1.0
CG A:HIS505 3.2 11.5 1.0
CB A:CYS500 3.2 12.3 1.0
CE1 A:HIS505 3.3 15.6 1.0
CB A:HIS505 3.5 12.3 1.0
SD A:MET510 3.5 15.7 1.0
O A:LEU442 3.6 17.1 1.0
CB A:HIS443 3.6 16.1 1.0
CA A:HIS443 3.7 15.4 1.0
CB A:LEU502 4.0 12.3 1.0
NE2 A:HIS443 4.2 20.5 1.0
CD2 A:HIS443 4.3 17.8 1.0
CE A:MET510 4.3 18.2 1.0
C A:LEU442 4.3 16.9 1.0
NE2 A:HIS505 4.4 15.6 1.0
CD2 A:HIS505 4.4 15.4 1.0
N A:HIS443 4.4 15.3 1.0
CD1 A:LEU502 4.6 13.9 1.0
CA A:CYS500 4.6 11.8 1.0
CG A:LEU502 4.8 12.3 1.0
C A:HIS443 4.9 15.2 1.0
CG A:MET510 4.9 15.2 1.0
O A:LEU502 5.0 11.3 1.0
CA A:HIS505 5.0 11.9 1.0
CD A:PRO444 5.0 14.2 1.0

Copper binding site 2 out of 4 in 1pf3

Go back to Copper Binding Sites List in 1pf3
Copper binding site 2 out of 4 in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo


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 the M441L Mutant of the Multicopper Oxidase Cueo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu703

b:17.0
occ:0.75
NE2 A:HIS101 1.9 12.5 1.0
NE2 A:HIS446 1.9 11.9 1.0
O A:HOH2018 2.8 14.8 1.0
CE1 A:HIS101 2.8 13.1 1.0
CD2 A:HIS446 2.9 11.9 1.0
CE1 A:HIS446 2.9 11.8 1.0
CD2 A:HIS101 3.0 10.2 1.0
CD2 A:HIS448 3.2 11.7 1.0
NE2 A:HIS448 3.3 11.5 1.0
CL A:C2C702 3.3 24.0 1.0
CG A:HIS103 3.5 8.7 1.0
ND1 A:HIS103 3.7 9.5 1.0
CA A:HIS103 3.7 9.4 1.0
CU2 A:C2C702 3.8 16.1 1.0
CB A:HIS103 3.8 8.5 1.0
CG A:HIS448 3.8 11.0 1.0
CE1 A:HIS448 3.9 12.6 1.0
ND1 A:HIS101 4.0 12.6 1.0
ND1 A:HIS446 4.0 12.3 1.0
CG A:HIS446 4.0 12.3 1.0
CD2 A:HIS103 4.0 10.7 1.0
CG A:HIS101 4.1 10.8 1.0
CU3 A:C2C702 4.2 13.8 1.0
CE1 A:HIS103 4.2 10.2 1.0
ND1 A:HIS448 4.2 11.2 1.0
N A:GLY104 4.4 11.4 1.0
NE2 A:HIS103 4.4 9.8 1.0
N A:HIS103 4.5 9.8 1.0
C A:HIS103 4.6 10.2 1.0
CA A:HIS448 4.6 11.4 1.0
CB A:HIS448 4.7 12.1 1.0
O A:HOH2058 4.8 17.8 1.0
O A:TRP102 4.8 11.5 1.0
O A:HOH2010 4.9 17.2 1.0
N A:HIS448 5.0 11.8 1.0

Copper binding site 3 out of 4 in 1pf3

Go back to Copper Binding Sites List in 1pf3
Copper binding site 3 out of 4 in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo


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 the M441L Mutant of the Multicopper Oxidase Cueo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:16.1
occ:1.00
CU2 A:C2C702 0.0 16.1 1.0
NE2 A:HIS448 1.9 11.5 1.0
NE2 A:HIS143 2.0 16.9 1.0
NE2 A:HIS499 2.0 12.2 1.0
CL A:C2C702 2.4 24.0 1.0
CE1 A:HIS448 2.8 12.6 1.0
CE1 A:HIS499 3.0 13.4 1.0
CD2 A:HIS499 3.0 11.1 1.0
CE1 A:HIS143 3.0 15.6 1.0
CD2 A:HIS143 3.0 13.6 1.0
CD2 A:HIS448 3.0 11.7 1.0
O A:HOH2324 3.7 26.3 1.0
CD2 A:HIS446 3.7 11.9 1.0
CU A:CU703 3.8 17.0 0.8
ND1 A:HIS448 4.0 11.2 1.0
NE2 A:HIS101 4.0 12.5 1.0
ND1 A:HIS499 4.1 11.5 1.0
CD2 A:HIS101 4.1 10.2 1.0
CG A:HIS499 4.1 11.3 1.0
CG A:HIS448 4.1 11.0 1.0
ND1 A:HIS143 4.1 16.2 1.0
CG A:HIS143 4.2 13.9 1.0
NE2 A:HIS446 4.2 11.9 1.0
CB A:MET497 4.4 11.9 1.0
CE1 A:HIS101 4.8 13.1 1.0
CG A:HIS101 4.8 10.8 1.0
CU3 A:C2C702 4.8 13.8 1.0
CG A:MET497 4.9 12.1 1.0
CG A:HIS446 4.9 12.3 1.0
OE1 A:GLU506 5.0 21.6 1.0

Copper binding site 4 out of 4 in 1pf3

Go back to Copper Binding Sites List in 1pf3
Copper binding site 4 out of 4 in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo


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 the M441L Mutant of the Multicopper Oxidase Cueo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:13.8
occ:1.00
CU3 A:C2C702 0.0 13.8 1.0
ND1 A:HIS103 2.0 9.5 1.0
NE2 A:HIS141 2.0 11.1 1.0
NE2 A:HIS501 2.1 11.1 1.0
CL A:C2C702 2.5 24.0 1.0
CE1 A:HIS103 2.9 10.2 1.0
CE1 A:HIS141 3.0 9.9 1.0
CD2 A:HIS141 3.0 9.5 1.0
CE1 A:HIS501 3.1 12.5 1.0
CG A:HIS103 3.1 8.7 1.0
CD2 A:HIS501 3.1 11.2 1.0
CB A:HIS103 3.5 8.5 1.0
CZ2 A:TRP139 3.7 10.7 1.0
CE2 A:TRP139 4.0 9.0 1.0
NE2 A:HIS103 4.1 9.8 1.0
ND1 A:HIS141 4.1 12.9 1.0
NE1 A:TRP139 4.1 9.3 1.0
O A:HOH2324 4.1 26.3 1.0
CG A:HIS141 4.2 9.9 1.0
CU A:CU703 4.2 17.0 0.8
CD2 A:HIS103 4.2 10.7 1.0
ND1 A:HIS501 4.2 10.4 1.0
CD2 A:HIS101 4.3 10.2 1.0
CG A:HIS501 4.3 10.6 1.0
CH2 A:TRP139 4.4 11.4 1.0
NE2 A:HIS446 4.5 11.9 1.0
CD2 A:HIS446 4.6 11.9 1.0
NE2 A:HIS101 4.6 12.5 1.0
CA A:HIS103 4.8 9.4 1.0
CU2 A:C2C702 4.8 16.1 1.0

Reference:

S.A.Roberts, G.F.Wildner, G.Grass, A.Weichsel, A.Ambrus, C.Rensing, W.R.Montfort. A Labile Regulatory Copper Ion Lies Near the T1 Copper Site in the Multicopper Oxidase Cueo. J.Biol.Chem. V. 278 31958 2003.
ISSN: ISSN 0021-9258
PubMed: 12794077
DOI: 10.1074/JBC.M302963200
Page generated: Sun Dec 13 11:01:20 2020

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