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4UMW

CRYSTAL STRUCTURE OF A ZINC-TRANSPORTING PIB-TYPE ATPASE IN E2.PI STATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0006829biological_processzinc ion transport
A0008551molecular_functionP-type cadmium transporter activity
A0015086molecular_functioncadmium ion transmembrane transporter activity
A0015662molecular_functionP-type ion transporter activity
A0016020cellular_componentmembrane
A0016463molecular_functionP-type zinc transporter activity
A0016887molecular_functionATP hydrolysis activity
A0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0070574biological_processcadmium ion transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ALF A 1731
ChainResidue
ATHR288
AASN631
AMG1732
AHOH2022
AGLY289
AASP436
ALYS437
ATHR438
ATHR583
AGLY584
ALYS610
AASP628

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1732
ChainResidue
AASP436
ATHR438
AASP628
AASP632
AALF1731
AHOH2022

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLADTGATVLVT
ChainResidueDetails
AVAL711-THR722

site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP436-THR442

site_idPS01047
Number of Residues30
DetailsHMA_1 Heavy-metal-associated domain. VsGMdCaACarkVEnaVrqlagvnqvq.VlF
ChainResidueDetails
AVAL54-PHE83

site_idPS01229
Number of Residues23
DetailsCOF_2 Hypothetical cof family signature 2. VGDGiNDapaMkaAaiGiaMgsG
ChainResidueDetails
AVAL626-GLY648

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues547
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-ARG124
AALA168-SER179
AARG223-PRO356
ATHR405-ASN685

site_idSWS_FT_FI2
Number of Residues153
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ALEU125-GLU145
APHE147-ILE167
ATYR180-ILE197
AALA203-SER222
AALA357-TRP377
AGLY384-ILE404
AILE686-LEU702
ATRP708-LEU729

site_idSWS_FT_FI3
Number of Residues14
DetailsTOPO_DOM: Periplasmic => ECO:0000305
ChainResidueDetails
AGLN146
AGLY198-GLU202
AGLN378-LYS383
AGLY703-LEU707

site_idSWS_FT_FI4
Number of Residues2
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P37617
ChainResidueDetails
AARG730-ARG732

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000305|PubMed:25132545
ChainResidueDetails
AASP436

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P37617
ChainResidueDetails
AASP58
ACYS392
ACYS394

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280
ChainResidueDetails
ACYS59
ACYS62

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25132545
ChainResidueDetails
AASP436
ATHR438
AASP628

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P37617, ECO:0000305|PubMed:25132545
ChainResidueDetails
AASP714

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Important for metal transport => ECO:0000305|PubMed:25132545
ChainResidueDetails
ALYS693

218853

PDB entries from 2024-04-24

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