Structure of PDB 1zpu Chain A

Receptor sequence
>1zpuA (length=529) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ETHTFNWTTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTN
GMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDYNVG
TYWYHSHTDGQYEDGMKGLFIIKDDSFPYDYDEELSLSLSEWYHDLVTDL
TKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVS
QYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNF
AIMQKFDDTMLDVIPSDLQLNATSYMVYNKTAALPTQNYVDSIDNFLDDF
YLQPYEKEAIYGEPDHVITVDVVMDNLKNGVNYAFFNNITYTAPKVPTLM
TVLSSGDQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHA
FQTIQRDRTYDDALGEVPHSFDPDNHPAFPEYPMRRDTLYVRPQSNFVIR
FKADNPGVWFFHCHIEWHLLQGLGLVLVEDPFGIQDAHSQQLSENHLEVC
QSCSVATEGNAAANTLDLTDLTGENVQHA
3D structure
PDB1zpu The copper-iron connection in biology: Structure of the metallo-oxidase Fet3p.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H81 H83 G84 Q87 H126 S127 H128 Q132 M137 H413 H416 H418 H483 C484 H485 I486 H489 L494
Catalytic site (residue number reindexed from 1) H60 H62 G63 Q66 H105 S106 H107 Q111 M116 H392 H395 H397 H462 C463 H464 I465 H468 L473
Enzyme Commision number 1.16.3.1: ferroxidase.
1.16.3.4: cuproxidase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 MAN A L40 Q189 N190 D288 Q290 L19 Q168 N169 D267 Q269
BS02 CU1 A H413 C484 H489 H392 C463 H468
BS03 CU1 A H128 H418 H483 H107 H397 H462
BS04 CU1 A H83 H126 H485 H62 H105 H464
BS05 CU1 A H81 H416 H418 H60 H395 H397
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0006811 monoatomic ion transport

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1zpu, PDBe:1zpu, PDBj:1zpu
PDBsum1zpu
PubMed16230618
UniProtP38993|FET3_YEAST Iron transport multicopper oxidase FET3 (Gene Name=FET3)

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