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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9RCV

Structure of the Human Peptide-Loading Complex Arrested by HCMV US6

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002250biological_processadaptive immune response
A0002376biological_processimmune system process
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006952biological_processdefense response
A0015031biological_processprotein transport
A0015433molecular_functionABC-type peptide antigen transporter activity
A0015440molecular_functionABC-type peptide transporter activity
A0015833biological_processpeptide transport
A0016020cellular_componentmembrane
A0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
A0023029molecular_functionMHC class Ib protein binding
A0030670cellular_componentphagocytic vesicle membrane
A0031090cellular_componentorganelle membrane
A0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
A0042287molecular_functionMHC protein binding
A0042288molecular_functionMHC class I protein binding
A0042605molecular_functionpeptide antigen binding
A0042803molecular_functionprotein homodimerization activity
A0042824cellular_componentMHC class I peptide loading complex
A0042825cellular_componentTAP complex
A0043531molecular_functionADP binding
A0046872molecular_functionmetal ion binding
A0046967biological_processcytosol to endoplasmic reticulum transport
A0046978molecular_functionTAP1 binding
A0046979molecular_functionTAP2 binding
A0055085biological_processtransmembrane transport
A1904680molecular_functionpeptide transmembrane transporter activity
E0000166molecular_functionnucleotide binding
E0002250biological_processadaptive immune response
E0002376biological_processimmune system process
E0002489biological_processantigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005783cellular_componentendoplasmic reticulum
E0005789cellular_componentendoplasmic reticulum membrane
E0006952biological_processdefense response
E0015031biological_processprotein transport
E0015433molecular_functionABC-type peptide antigen transporter activity
E0015440molecular_functionABC-type peptide transporter activity
E0015833biological_processpeptide transport
E0016020cellular_componentmembrane
E0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
E0023029molecular_functionMHC class Ib protein binding
E0030670cellular_componentphagocytic vesicle membrane
E0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
E0042605molecular_functionpeptide antigen binding
E0042824cellular_componentMHC class I peptide loading complex
E0042825cellular_componentTAP complex
E0046872molecular_functionmetal ion binding
E0046967biological_processcytosol to endoplasmic reticulum transport
E0046968biological_processpeptide antigen transport
E0046978molecular_functionTAP1 binding
E0046980molecular_functiontapasin binding
E0055085biological_processtransmembrane transport
E1904680molecular_functionpeptide transmembrane transporter activity
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQAVALARAL
ChainResidueDetails
ALEU643-LEU657
ELEU607-LEU621
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH
ChainResidueDetails
CTYR257-HIS263
DTYR78-HIS84
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues119
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues276
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues566
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues239
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues186
DetailsRegion: {"description":"Part of the peptide-binding site","evidences":[{"source":"PubMed","id":"8955196","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P36370","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11532960","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JJ7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P36370","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsSite: {"description":"Inter-subunit salt bridge with TAPBP","evidences":[{"source":"PubMed","id":"26611325","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsSite: {"description":"May be involved in interaction with TAP"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues176
DetailsDomain: {"description":"Ig-like C1-type"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid; in form pI 5.3","evidences":[{"source":"PubMed","id":"7554280","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-01-28

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