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7L9X

Structure of VPS4B in complex with an allele-specific covalent inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000922cellular_componentspindle pole
A0001525biological_processangiogenesis
A0001778biological_processplasma membrane repair
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005643cellular_componentnuclear pore
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006813biological_processpotassium ion transport
A0006914biological_processautophagy
A0006997biological_processnucleus organization
A0007032biological_processendosome organization
A0007033biological_processvacuole organization
A0007034biological_processvacuolar transport
A0007080biological_processmitotic metaphase chromosome alignment
A0007417biological_processcentral nervous system development
A0010008cellular_componentendosome membrane
A0010824biological_processregulation of centrosome duplication
A0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016197biological_processendosomal transport
A0016236biological_processmacroautophagy
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0030301biological_processcholesterol transport
A0030496cellular_componentmidbody
A0031468biological_processnuclear membrane reassembly
A0031902cellular_componentlate endosome membrane
A0032510biological_processendosome to lysosome transport via multivesicular body sorting pathway
A0033993biological_processresponse to lipid
A0036258biological_processmultivesicular body assembly
A0039702biological_processviral budding via host ESCRT complex
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043162biological_processubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway
A0044877molecular_functionprotein-containing complex binding
A0046761biological_processviral budding from plasma membrane
A0051261biological_processprotein depolymerization
A0051301biological_processcell division
A0060070biological_processcanonical Wnt signaling pathway
A0060856biological_processestablishment of blood-brain barrier
A0061738biological_processlate endosomal microautophagy
A0061764biological_processlate endosome to lysosome transport via multivesicular body sorting pathway
A0061952biological_processmidbody abscission
A0070062cellular_componentextracellular exosome
A0071985biological_processmultivesicular body sorting pathway
A0090148biological_processmembrane fission
A0090543cellular_componentFlemming body
A0090611biological_processubiquitin-independent protein catabolic process via the multivesicular body sorting pathway
A0097352biological_processautophagosome maturation
A1901673biological_processregulation of mitotic spindle assembly
A1903542biological_processnegative regulation of exosomal secretion
A1903543biological_processpositive regulation of exosomal secretion
A1903724biological_processpositive regulation of centriole elongation
A1904903biological_processESCRT III complex disassembly
A1904949cellular_componentATPase complex
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue XQV A 501
ChainResidue
ACYS135
AGLY338
AALA339
ASO4502
AALA137
AGLY177
ATHR178
AGLY179
ATYR182
AMET309
ALEU312
AHIS313

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 502
ChainResidue
AGLY177
ATHR178
AGLY179
ALYS180
ASER181
AXQV501
AHOH605

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues20
DetailsAAA AAA-protein family signature. IlVLgATNipwvLDsAIrrR
ChainResidueDetails
AILE272-ARG291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY174

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER93
ASER108

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER102

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER410

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PDB entries from 2024-07-10

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