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1R7R

The crystal structure of murine p97/VCP at 3.6A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000502cellular_componentproteasome complex
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006511biological_processubiquitin-dependent protein catabolic process
A0006734biological_processNADH metabolic process
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0006914biological_processautophagy
A0006974biological_processDNA damage response
A0008289molecular_functionlipid binding
A0010494cellular_componentcytoplasmic stress granule
A0010498biological_processproteasomal protein catabolic process
A0010918biological_processpositive regulation of mitochondrial membrane potential
A0016236biological_processmacroautophagy
A0016567biological_processprotein ubiquitination
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0019079biological_processviral genome replication
A0019903molecular_functionprotein phosphatase binding
A0019904molecular_functionprotein domain specific binding
A0019985biological_processtranslesion synthesis
A0030970biological_processretrograde protein transport, ER to cytosol
A0031334biological_processpositive regulation of protein-containing complex assembly
A0031593molecular_functionpolyubiquitin modification-dependent protein binding
A0031625molecular_functionubiquitin protein ligase binding
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032510biological_processendosome to lysosome transport via multivesicular body sorting pathway
A0032991cellular_componentprotein-containing complex
A0034098cellular_componentVCP-NPL4-UFD1 AAA ATPase complex
A0034605biological_processcellular response to heat
A0035617biological_processstress granule disassembly
A0035800molecular_functiondeubiquitinase activator activity
A0035861cellular_componentsite of double-strand break
A0036297biological_processinterstrand cross-link repair
A0036435molecular_functionK48-linked polyubiquitin modification-dependent protein binding
A0036503biological_processERAD pathway
A0036513cellular_componentDerlin-1 retrotranslocation complex
A0042288molecular_functionMHC class I protein binding
A0042802molecular_functionidentical protein binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0043209cellular_componentmyelin sheath
A0043531molecular_functionADP binding
A0044389molecular_functionubiquitin-like protein ligase binding
A0044877molecular_functionprotein-containing complex binding
A0045202cellular_componentsynapse
A0045732biological_processpositive regulation of protein catabolic process
A0045879biological_processnegative regulation of smoothened signaling pathway
A0046034biological_processATP metabolic process
A0048471cellular_componentperinuclear region of cytoplasm
A0050807biological_processregulation of synapse organization
A0051228biological_processmitotic spindle disassembly
A0061857biological_processendoplasmic reticulum stress-induced pre-emptive quality control
A0070842biological_processaggresome assembly
A0071218biological_processcellular response to misfolded protein
A0072389biological_processflavin adenine dinucleotide catabolic process
A0090263biological_processpositive regulation of canonical Wnt signaling pathway
A0097352biological_processautophagosome maturation
A0098978cellular_componentglutamatergic synapse
A0106300biological_processprotein-DNA covalent cross-linking repair
A0120186biological_processnegative regulation of protein localization to chromatin
A0140036molecular_functionubiquitin-modified protein reader activity
A1901224biological_processpositive regulation of non-canonical NF-kappaB signal transduction
A1903006biological_processpositive regulation of protein K63-linked deubiquitination
A1903715biological_processregulation of aerobic respiration
A1903843biological_processcellular response to arsenite ion
A1903862biological_processpositive regulation of oxidative phosphorylation
A1904288molecular_functionBAT3 complex binding
A1904949cellular_componentATPase complex
A1905634biological_processregulation of protein localization to chromatin
A1990381molecular_functionubiquitin-specific protease binding
A1990730cellular_componentVCP-NSFL1C complex
A2000060biological_processpositive regulation of ubiquitin-dependent protein catabolic process
A2001171biological_processpositive regulation of ATP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP A 817
ChainResidue
AASP205
AHIS384
AGLY408
AALA409
AVAL206
AGLY207
AGLY248
ATHR249
AGLY250
ATHR252
ALEU253
AARG359

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R
ChainResidueDetails
AVAL341-ARG359
AVAL617-ARG635

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:11163219, ECO:0000305|PubMed:14988733
ChainResidueDetails
APRO247
AHIS384
AGLY521

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
AASN348

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
ASER3
ASER7
ASER13
ASER37
ASER462
ASER702
ASER775
ASER787

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820
ChainResidueDetails
ALYS315

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
ATHR436

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS502
ALYS505
ALYS754

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS668

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER770

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR805

site_idSWS_FT_FI11
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
ALYS8
ALYS18

219140

PDB entries from 2024-05-01

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