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4P6Z

Crystal structure of the human BST2 cytoplasmic domain and the HIV-1 Vpu cytoplasmic domain bound to the clathrin adaptor protein complex 1 (AP1) core

Functional Information from GO Data
ChainGOidnamespacecontents
B0006886biological_processintracellular protein transport
B0015031biological_processprotein transport
B0016192biological_processvesicle-mediated transport
B0030117cellular_componentmembrane coat
B0030276molecular_functionclathrin binding
G0005794cellular_componentGolgi apparatus
G0006886biological_processintracellular protein transport
G0016192biological_processvesicle-mediated transport
G0030117cellular_componentmembrane coat
G0030121cellular_componentAP-1 adaptor complex
M0005515molecular_functionprotein binding
M0005765cellular_componentlysosomal membrane
M0005769cellular_componentearly endosome
M0005794cellular_componentGolgi apparatus
M0005802cellular_componenttrans-Golgi network
M0005829cellular_componentcytosol
M0006886biological_processintracellular protein transport
M0006896biological_processGolgi to vacuole transport
M0015031biological_processprotein transport
M0016192biological_processvesicle-mediated transport
M0030121cellular_componentAP-1 adaptor complex
M0030131cellular_componentclathrin adaptor complex
M0030665cellular_componentclathrin-coated vesicle membrane
M0031410cellular_componentcytoplasmic vesicle
M0032438biological_processmelanosome organization
M0032588cellular_componenttrans-Golgi network membrane
M0035615molecular_functionclathrin-cargo adaptor activity
M0035646biological_processendosome to melanosome transport
M0045202cellular_componentsynapse
M0060155biological_processplatelet dense granule organization
M1903232biological_processmelanosome assembly
S0000139cellular_componentGolgi membrane
S0005515molecular_functionprotein binding
S0005765cellular_componentlysosomal membrane
S0005769cellular_componentearly endosome
S0005794cellular_componentGolgi apparatus
S0005829cellular_componentcytosol
S0005905cellular_componentclathrin-coated pit
S0006886biological_processintracellular protein transport
S0006898biological_processreceptor-mediated endocytosis
S0009615biological_processresponse to virus
S0015031biological_processprotein transport
S0016020cellular_componentmembrane
S0016192biological_processvesicle-mediated transport
S0030117cellular_componentmembrane coat
S0030121cellular_componentAP-1 adaptor complex
S0030659cellular_componentcytoplasmic vesicle membrane
S0031410cellular_componentcytoplasmic vesicle
S0032588cellular_componenttrans-Golgi network membrane
S0035615molecular_functionclathrin-cargo adaptor activity
S0043195cellular_componentterminal bouton
S0060155biological_processplatelet dense granule organization
S0098793cellular_componentpresynapse
S0110010biological_processbasolateral protein secretion
S1903232biological_processmelanosome assembly
V0005261molecular_functionmonoatomic cation channel activity
V0019076biological_processviral release from host cell
V0032801biological_processreceptor catabolic process
V0033644cellular_componenthost cell membrane
V0042609molecular_functionCD4 receptor binding
Functional Information from PROSITE/UniProt
site_idPS00989
Number of Residues11
DetailsCLAT_ADAPTOR_S Clathrin adaptor complexes small chain signature. VVYKryasLYF
ChainResidueDetails
SVAL57-PHE67

site_idPS00990
Number of Residues21
DetailsCLAT_ADAPTOR_M_1 Clathrin adaptor complexes medium chain signature 1. VSWRse.GikYrkNeVFLDVIE
ChainResidueDetails
MVAL157-GLU177

site_idPS00991
Number of Residues15
DetailsCLAT_ADAPTOR_M_2 Clathrin adaptor complexes medium chain signature 2. IsFIPPdGeFeLmsY
ChainResidueDetails
MILE253-TYR267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues253
DetailsDomain: {"description":"MHD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00404","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"Q9BXS5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q32Q06","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"O35643","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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