Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ZPU

Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0006811biological_processmonoatomic ion transport
A0016491molecular_functionoxidoreductase activity
B0005507molecular_functioncopper ion binding
B0006811biological_processmonoatomic ion transport
B0016491molecular_functionoxidoreductase activity
C0005507molecular_functioncopper ion binding
C0006811biological_processmonoatomic ion transport
C0016491molecular_functionoxidoreductase activity
D0005507molecular_functioncopper ion binding
D0006811biological_processmonoatomic ion transport
D0016491molecular_functionoxidoreductase activity
E0005507molecular_functioncopper ion binding
E0006811biological_processmonoatomic ion transport
E0016491molecular_functionoxidoreductase activity
F0005507molecular_functioncopper ion binding
F0006811biological_processmonoatomic ion transport
F0016491molecular_functionoxidoreductase activity
Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GtYwYhShTDgqYeDGMkglF
ChainResidueDetails
AGLY121-PHE141
AGLY478-LEU498

site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHiewHllqGL
ChainResidueDetails
AHIS483-LEU494

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues684
DetailsDomain: {"description":"Plastocyanin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues864
DetailsDomain: {"description":"Plastocyanin-like 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues840
DetailsDomain: {"description":"Plastocyanin-like 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"16230618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZPU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues36
DetailsBinding site: {"description":"type 3 copper site","evidences":[{"source":"PubMed","id":"16230618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZPU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues18
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"16230618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZPU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues66
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16230618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZPU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
AHIS485
ACYS484
AHIS483

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
BHIS485
BCYS484
BHIS483

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
CHIS485
CCYS484
CHIS483

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
DHIS485
DCYS484
DHIS483

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
EHIS485
ECYS484
EHIS483

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
FHIS485
FCYS484
FHIS483

248942

PDB entries from 2026-02-11

PDB statisticsPDBj update infoContact PDBjnumon