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Copper in PDB 1zpu: Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import

Protein crystallography data

The structure of Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import, PDB code: 1zpu was solved by A.B.Taylor, C.S.Stoj, L.Ziegler, D.J.Kosman, P.J.Hart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.80
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 168.534, 168.534, 174.605, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 25.7

Copper Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Copper atom in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import (pdb code 1zpu). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 24 binding sites of Copper where determined in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import, PDB code: 1zpu:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 24 in 1zpu

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Copper binding site 1 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


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 FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:82.5
occ:1.00
ND1 A:HIS413 2.1 70.1 1.0
ND1 A:HIS489 2.1 67.2 1.0
SG A:CYS484 2.2 70.5 1.0
CG A:HIS413 3.0 69.2 1.0
CE1 A:HIS489 3.1 65.9 1.0
CG A:HIS489 3.1 67.9 1.0
CE1 A:HIS413 3.1 70.7 1.0
CB A:HIS413 3.3 68.7 1.0
CB A:CYS484 3.4 69.0 1.0
CB A:HIS489 3.4 68.1 1.0
CD1 A:ILE486 3.7 66.8 1.0
CD1 A:LEU494 3.8 68.8 1.0
CA A:HIS413 4.0 69.0 1.0
CB A:ILE486 4.1 69.0 1.0
CD2 A:HIS413 4.2 69.8 1.0
NE2 A:HIS489 4.2 64.8 1.0
NE2 A:HIS413 4.2 70.4 1.0
CD2 A:HIS489 4.2 66.1 1.0
CG1 A:ILE486 4.3 67.8 1.0
CD A:PRO414 4.6 69.3 1.0
O A:THR412 4.7 70.1 1.0
CA A:CYS484 4.7 69.2 1.0
CG2 A:ILE486 4.8 68.8 1.0
CA A:HIS489 4.9 68.5 1.0
C A:HIS413 5.0 69.3 1.0
CE A:MET345 5.0 73.6 1.0
N A:HIS413 5.0 69.4 1.0

Copper binding site 2 out of 24 in 1zpu

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Copper binding site 2 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


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 FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1002

b:87.4
occ:1.00
NE2 A:HIS128 2.1 70.3 1.0
NE2 A:HIS418 2.1 69.0 1.0
NE2 A:HIS483 2.2 70.6 1.0
CE1 A:HIS128 2.9 70.7 1.0
CE1 A:HIS418 3.0 69.7 1.0
CD2 A:HIS483 3.1 70.2 1.0
CE1 A:HIS483 3.2 70.8 1.0
CD2 A:HIS128 3.2 70.5 1.0
CD2 A:HIS418 3.2 69.8 1.0
ND1 A:HIS128 4.1 70.5 1.0
ND1 A:HIS418 4.2 68.9 1.0
CD2 A:PHE481 4.2 68.7 1.0
CG A:HIS483 4.2 69.7 1.0
CD2 A:HIS416 4.2 67.7 1.0
CG A:HIS128 4.2 69.9 1.0
ND1 A:HIS483 4.3 70.0 1.0
CG A:HIS418 4.3 69.0 1.0
CD2 A:HIS81 4.3 68.6 1.0
NE2 A:HIS81 4.5 68.3 1.0
CB A:PHE481 4.5 68.8 1.0
CU A:CU11004 4.6 0.0 1.0
CG2 A:VAL96 4.6 68.0 1.0
CG A:PHE481 4.7 68.6 1.0
NE2 A:HIS416 4.8 67.4 1.0

Copper binding site 3 out of 24 in 1zpu

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Copper binding site 3 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


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 FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1003

b:89.2
occ:1.00
ND1 A:HIS83 1.9 68.0 1.0
NE2 A:HIS126 2.1 66.8 1.0
NE2 A:HIS485 2.2 65.8 1.0
CE1 A:HIS83 2.9 69.0 1.0
CD2 A:HIS126 2.9 67.2 1.0
CG A:HIS83 3.0 68.9 1.0
CE1 A:HIS126 3.1 68.3 1.0
CE1 A:HIS485 3.1 67.5 1.0
CD2 A:HIS485 3.2 66.5 1.0
CB A:HIS83 3.4 68.5 1.0
CZ2 A:TRP124 3.8 66.6 1.0
CD2 A:HIS81 3.8 68.6 1.0
NE2 A:HIS83 4.0 69.1 1.0
CU A:CU11004 4.1 0.0 1.0
CD2 A:HIS83 4.1 69.0 1.0
CG A:HIS126 4.1 68.3 1.0
ND1 A:HIS126 4.2 68.9 1.0
NE2 A:HIS81 4.2 68.3 1.0
CE2 A:TRP124 4.2 66.6 1.0
ND1 A:HIS485 4.3 67.5 1.0
CG A:HIS485 4.4 67.2 1.0
CH2 A:TRP124 4.4 67.3 1.0
CD2 A:HIS416 4.4 67.7 1.0
CA A:HIS83 4.4 68.9 1.0
NE1 A:TRP124 4.5 67.5 1.0
NE2 A:HIS416 4.5 67.4 1.0
CB A:ALA254 4.6 68.5 1.0

Copper binding site 4 out of 24 in 1zpu

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Copper binding site 4 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


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 FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1004

b:0.0
occ:1.00
NE2 A:HIS416 2.1 67.4 1.0
NE2 A:HIS81 2.1 68.3 1.0
CE1 A:HIS81 2.9 68.0 1.0
CE1 A:HIS416 3.0 67.5 1.0
CD2 A:HIS416 3.1 67.7 1.0
CD2 A:HIS81 3.2 68.6 1.0
NE2 A:HIS418 3.5 69.0 1.0
CE1 A:HIS418 3.6 69.7 1.0
CD2 A:HIS418 3.6 69.8 1.0
ND1 A:HIS83 3.6 68.0 1.0
CA A:HIS83 3.7 68.9 1.0
CG A:HIS83 3.7 68.9 1.0
ND1 A:HIS418 3.8 68.9 1.0
CG A:HIS418 3.8 69.0 1.0
N A:GLY84 3.8 69.2 1.0
CE1 A:HIS83 4.0 69.0 1.0
ND1 A:HIS81 4.1 69.2 1.0
CU A:CU11003 4.1 89.2 1.0
ND1 A:HIS416 4.1 67.8 1.0
CB A:HIS83 4.1 68.5 1.0
CD2 A:HIS83 4.1 69.0 1.0
CG A:HIS416 4.2 68.5 1.0
C A:HIS83 4.3 69.1 1.0
CG A:HIS81 4.3 69.1 1.0
NE2 A:HIS83 4.3 69.1 1.0
CA A:HIS418 4.5 69.0 1.0
CU A:CU11002 4.6 87.4 1.0
N A:HIS83 4.7 69.0 1.0
CB A:HIS418 4.7 68.7 1.0
O A:PHE82 4.8 69.2 1.0
CA A:GLY84 4.9 69.2 1.0
N A:HIS418 5.0 69.1 1.0

Copper binding site 5 out of 24 in 1zpu

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Copper binding site 5 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1001

b:87.1
occ:1.00
ND1 B:HIS489 2.0 66.9 1.0
ND1 B:HIS413 2.1 70.1 1.0
SG B:CYS484 2.2 70.3 1.0
CE1 B:HIS489 2.9 67.7 1.0
CG B:HIS413 3.0 68.9 1.0
CE1 B:HIS413 3.1 70.9 1.0
CG B:HIS489 3.1 67.8 1.0
CB B:HIS413 3.3 68.9 1.0
CB B:CYS484 3.4 69.2 1.0
CB B:HIS489 3.5 68.1 1.0
CD1 B:ILE486 3.6 68.1 1.0
CA B:HIS413 3.9 68.9 1.0
CD1 B:LEU494 3.9 68.6 1.0
NE2 B:HIS489 4.1 66.3 1.0
CB B:ILE486 4.1 68.7 1.0
CD2 B:HIS413 4.2 69.5 1.0
NE2 B:HIS413 4.2 70.9 1.0
CD2 B:HIS489 4.2 66.8 1.0
CG1 B:ILE486 4.2 68.0 1.0
O B:THR412 4.7 70.0 1.0
CD B:PRO414 4.7 69.2 1.0
CA B:CYS484 4.8 69.2 1.0
CG2 B:ILE486 4.8 68.1 1.0
N B:HIS413 4.9 69.3 1.0
C B:HIS413 4.9 69.3 1.0
CA B:HIS489 5.0 68.5 1.0

Copper binding site 6 out of 24 in 1zpu

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Copper binding site 6 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:88.8
occ:1.00
NE2 B:HIS418 2.0 69.0 1.0
NE2 B:HIS483 2.1 70.6 1.0
NE2 B:HIS128 2.2 69.3 1.0
CE1 B:HIS418 2.8 69.8 1.0
CE1 B:HIS483 3.0 70.8 1.0
CE1 B:HIS128 3.1 69.8 1.0
CD2 B:HIS483 3.1 69.8 1.0
CD2 B:HIS418 3.2 70.3 1.0
CD2 B:HIS128 3.2 70.2 1.0
CD2 B:HIS416 4.0 67.2 1.0
ND1 B:HIS418 4.0 70.7 1.0
ND1 B:HIS483 4.1 70.5 1.0
CD2 B:PHE481 4.1 68.7 1.0
CG B:HIS483 4.2 69.3 1.0
CG B:HIS418 4.2 69.8 1.0
ND1 B:HIS128 4.2 70.2 1.0
CG B:HIS128 4.3 69.6 1.0
CB B:PHE481 4.5 68.6 1.0
NE2 B:HIS416 4.5 67.2 1.0
CD2 B:HIS81 4.5 67.9 1.0
CU B:CU11004 4.5 0.0 1.0
NE2 B:HIS81 4.6 67.7 1.0
CG2 B:VAL96 4.7 68.5 1.0
CG B:PHE481 4.8 68.8 1.0
NE2 B:HIS485 5.0 63.9 1.0

Copper binding site 7 out of 24 in 1zpu

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Copper binding site 7 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1003

b:87.2
occ:1.00
ND1 B:HIS83 2.0 69.3 1.0
NE2 B:HIS126 2.0 69.0 1.0
NE2 B:HIS485 2.0 63.9 1.0
CE1 B:HIS83 2.8 70.0 1.0
CE1 B:HIS485 2.9 66.9 1.0
CD2 B:HIS126 2.9 68.6 1.0
CE1 B:HIS126 3.0 69.0 1.0
CG B:HIS83 3.1 68.8 1.0
CD2 B:HIS485 3.1 64.9 1.0
CB B:HIS83 3.6 68.7 1.0
CZ2 B:TRP124 3.7 66.3 1.0
NE2 B:HIS83 4.0 70.1 1.0
ND1 B:HIS485 4.0 66.2 1.0
CD2 B:HIS81 4.1 67.9 1.0
CG B:HIS126 4.1 68.3 1.0
ND1 B:HIS126 4.1 69.0 1.0
CE2 B:TRP124 4.1 67.2 1.0
CD2 B:HIS83 4.1 70.0 1.0
CU B:CU11004 4.2 0.0 1.0
CG B:HIS485 4.2 65.9 1.0
NE1 B:TRP124 4.3 67.1 1.0
CH2 B:TRP124 4.4 66.8 1.0
CB B:ALA254 4.4 68.7 1.0
CD2 B:HIS416 4.4 67.2 1.0
NE2 B:HIS416 4.4 67.2 1.0
NE2 B:HIS81 4.5 67.7 1.0
CA B:HIS83 4.6 68.8 1.0

Copper binding site 8 out of 24 in 1zpu

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Copper binding site 8 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1004

b:0.0
occ:1.00
NE2 B:HIS416 2.0 67.2 1.0
NE2 B:HIS81 2.1 67.7 1.0
CE1 B:HIS416 2.8 66.8 1.0
CE1 B:HIS81 3.0 67.8 1.0
CD2 B:HIS416 3.1 67.2 1.0
CD2 B:HIS81 3.2 67.9 1.0
CE1 B:HIS418 3.5 69.8 1.0
NE2 B:HIS418 3.5 69.0 1.0
CA B:HIS83 3.6 68.8 1.0
ND1 B:HIS83 3.6 69.3 1.0
CG B:HIS83 3.6 68.8 1.0
ND1 B:HIS418 3.7 70.7 1.0
CD2 B:HIS418 3.7 70.3 1.0
N B:GLY84 3.8 69.2 1.0
CG B:HIS418 3.8 69.8 1.0
ND1 B:HIS416 4.0 67.9 1.0
CE1 B:HIS83 4.0 70.0 1.0
CB B:HIS83 4.0 68.7 1.0
CD2 B:HIS83 4.1 70.0 1.0
CG B:HIS416 4.1 68.4 1.0
ND1 B:HIS81 4.1 69.5 1.0
CU B:CU11003 4.2 87.2 1.0
C B:HIS83 4.2 69.1 1.0
CG B:HIS81 4.3 69.7 1.0
NE2 B:HIS83 4.3 70.1 1.0
CU B:CU11002 4.5 88.8 1.0
CA B:HIS418 4.6 69.2 1.0
N B:HIS83 4.6 68.9 1.0
CB B:HIS418 4.7 68.9 1.0
O B:PHE82 4.8 69.1 1.0
CA B:GLY84 4.8 69.3 1.0
C B:PHE82 5.0 69.0 1.0

Copper binding site 9 out of 24 in 1zpu

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Copper binding site 9 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1001

b:85.4
occ:1.00
ND1 C:HIS489 2.1 67.5 1.0
ND1 C:HIS413 2.2 69.8 1.0
SG C:CYS484 2.2 69.8 1.0
CG C:HIS413 3.0 69.4 1.0
CE1 C:HIS489 3.0 67.5 1.0
CG C:HIS489 3.2 67.8 1.0
CB C:HIS413 3.2 69.2 1.0
CE1 C:HIS413 3.3 70.5 1.0
CB C:CYS484 3.3 69.0 1.0
CB C:HIS489 3.5 68.2 1.0
CD1 C:ILE486 3.7 68.0 1.0
CD1 C:LEU494 3.8 68.6 1.0
CA C:HIS413 3.9 69.1 1.0
NE2 C:HIS489 4.2 67.2 1.0
CB C:ILE486 4.2 68.5 1.0
CD2 C:HIS413 4.2 69.5 1.0
CG1 C:ILE486 4.2 68.0 1.0
CD2 C:HIS489 4.3 67.5 1.0
NE2 C:HIS413 4.3 70.5 1.0
CD C:PRO414 4.6 69.0 1.0
O C:THR412 4.6 70.1 1.0
CA C:CYS484 4.7 69.2 1.0
C C:HIS413 4.9 69.2 1.0
N C:HIS413 5.0 69.4 1.0

Copper binding site 10 out of 24 in 1zpu

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Copper binding site 10 out of 24 in the Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Crystal Structure of FET3P, A Multicopper Oxidase That Functions in Iron Import within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1002

b:85.4
occ:1.00
NE2 C:HIS483 2.0 69.4 1.0
NE2 C:HIS128 2.2 69.7 1.0
NE2 C:HIS418 2.2 69.9 1.0
CE1 C:HIS483 2.9 69.9 1.0
CD2 C:HIS483 3.0 69.2 1.0
CE1 C:HIS128 3.0 70.0 1.0
CE1 C:HIS418 3.1 70.0 1.0
CD2 C:HIS128 3.2 69.8 1.0
CD2 C:HIS418 3.3 69.9 1.0
CD2 C:HIS416 4.0 68.1 1.0
ND1 C:HIS483 4.0 69.9 1.0
CG C:HIS483 4.1 69.5 1.0
CD2 C:PHE481 4.2 68.1 1.0
ND1 C:HIS128 4.2 70.2 1.0
ND1 C:HIS418 4.3 68.9 1.0
CG C:HIS128 4.3 69.4 1.0
CG C:HIS418 4.4 69.0 1.0
CU C:CU11004 4.4 0.0 1.0
CB C:PHE481 4.5 68.7 1.0
CD2 C:HIS81 4.6 68.8 1.0
NE2 C:HIS416 4.7 67.6 1.0
NE2 C:HIS81 4.7 68.5 1.0
CG C:PHE481 4.8 68.4 1.0
CG2 C:VAL96 4.8 68.5 1.0
NE2 C:HIS485 5.0 64.5 1.0

Reference:

A.B.Taylor, C.S.Stoj, L.Ziegler, D.J.Kosman, P.J.Hart. The Copper-Iron Connection in Biology: Structure of the Metallo-Oxidase FET3P. Proc.Natl.Acad.Sci.Usa V. 102 15459 2005.
ISSN: ISSN 0027-8424
PubMed: 16230618
DOI: 10.1073/PNAS.0506227102
Page generated: Mon Jul 14 00:41:16 2025

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