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4UMV

CRYSTAL STRUCTURE OF A ZINC-TRANSPORTING PIB-TYPE ATPASE IN THE E2P 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
A0022857molecular_functiontransmembrane transporter activity
A0030001biological_processmetal ion transport
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0070574biological_processcadmium ion transmembrane transport
A0071577biological_processzinc ion transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1731
ChainResidue
AASP436
ATHR438
AASP628
AGLY629
ABEF1732

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEF A 1732
ChainResidue
ATHR583
AASP628
AASN631
AMG1731
ASER285
AGLY289
AASP436
ATHR438

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 Residues14
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues133
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues424
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"PubMed","id":"25132545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P37617","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25132545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P37617","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"25132545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Important for metal transport","evidences":[{"source":"PubMed","id":"25132545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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