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3IWL

Crystal structure of cisplatin bound to a human copper chaperone (monomer)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006825biological_processcopper ion transport
A0006878biological_processintracellular copper ion homeostasis
A0006979biological_processresponse to oxidative stress
A0016530molecular_functionmetallochaperone activity
A0016531molecular_functioncopper chaperone activity
A0032767molecular_functioncopper-dependent protein binding
A0046872molecular_functionmetal ion binding
A1903136molecular_functioncuprous ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PT A 69
ChainResidue
ATHR11
ACYS12
ACYS15
ATCE71

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 70
ChainResidue
AHOH80
AGLY27
AGLY28
AHIS46
ASER47
ATHR50

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TCE A 71
ChainResidue
ATHR11
ACYS12
AGLY14
ACYS15
ALYS60
APT69
AHOH129
AHOH152
AHOH156

Functional Information from PROSITE/UniProt
site_idPS01047
Number of Residues29
DetailsHMA_1 Heavy-metal-associated domain. SvDMtCgGCaeaVSrvLnklggvkyd..IdL
ChainResidueDetails
ASER7-LEU35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:31283225, ECO:0007744|PDB:5T7L
ChainResidueDetails
ACYS12
ACYS15

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08997
ChainResidueDetails
ALYS60

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PDB entries from 2024-07-24

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