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4YEA

Crystal structure of cisplatin bound to a human copper chaperone (dimer) - new refinement

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
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006825biological_processcopper ion transport
B0006878biological_processintracellular copper ion homeostasis
B0006979biological_processresponse to oxidative stress
B0016530molecular_functionmetallochaperone activity
B0016531molecular_functioncopper chaperone activity
B0032767molecular_functioncopper-dependent protein binding
B0046872molecular_functionmetal ion binding
B1903136molecular_functioncuprous ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 400
ChainResidue
ACYS12
ACYS15
BCYS12
BCYS15

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 401
ChainResidue
AHIS46
ASER47
ATHR50

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 B 101
ChainResidue
BHOH263
BGLY28
BHOH257

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 B 102
ChainResidue
BHIS46
BSER47
BTHR50

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 Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:31283225, ECO:0007744|PDB:5T7L
ChainResidueDetails
ACYS12
ACYS15
BCYS12
BCYS15

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER47
BSER47

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08997
ChainResidueDetails
ALYS60
BLYS60

221371

PDB entries from 2024-06-19

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