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7XUK

Structure of ATP7B C983S/C985S/D1027A mutant in presence of ATOX1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005375molecular_functioncopper ion transmembrane transporter activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005768cellular_componentendosome
A0005770cellular_componentlate endosome
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006812biological_processmonoatomic cation transport
A0006825biological_processcopper ion transport
A0006878biological_processintracellular copper ion homeostasis
A0006882biological_processintracellular zinc ion homeostasis
A0007595biological_processlactation
A0015677biological_processcopper ion import
A0015680biological_processprotein maturation by copper ion transfer
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
A0031410cellular_componentcytoplasmic vesicle
A0032588cellular_componenttrans-Golgi network membrane
A0034220biological_processmonoatomic ion transmembrane transport
A0035434biological_processcopper ion transmembrane transport
A0043682molecular_functionP-type divalent copper transporter activity
A0046688biological_processresponse to copper ion
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0051208biological_processsequestering of calcium ion
A0051649biological_processestablishment of localization in cell
A0060003biological_processcopper ion export
A0140581molecular_functionP-type monovalent copper transporter activity
A1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
Functional Information from PROSITE/UniProt
site_idPS01047
Number of Residues30
DetailsHMA_1 Heavy-metal-associated domain. IlGMtCqSCvksIEdrIsnlkgiismk.VsL
ChainResidueDetails
AILE64-LEU93
AVAL149-LEU178
AILE263-LEU292
AILE365-LEU394
AILE494-LEU523
AILE570-LEU599

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1211
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AVAL995-ARG1322
AMET1-SER653
AALA718-HIS724
ASER786-ARG919
AGLN1372-ILE1465

site_idSWS_FT_FI2
Number of Residues159
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
APHE920-ILE942
AGLN973-ALA994
AILE1323-ALA1340
APHE654-SER675
AILE698-GLN717
AARG725-LEU745
AASP765-LYS785
APRO1352-LEU1371

site_idSWS_FT_FI3
Number of Residues78
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AGLY943-PHE972
AASN676-LEU697
AVAL746-PHE764
AGLY1341-GLN1351

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250
ChainResidueDetails
AALA1027

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459
ChainResidueDetails
ACYS69
ACYS72
ACYS154
ACYS157
ACYS268
ACYS271
ACYS370
ACYS373
ACYS499
ACYS502
ACYS575
ACYS578

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP1267
AASP1271

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER23
ASER478

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64535
ChainResidueDetails
ASER481
ASER1398

221051

PDB entries from 2024-06-12

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