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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1R7R

The crystal structure of murine p97/VCP at 3.6A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000153cellular_componentcytoplasmic ubiquitin ligase complex
A0000423biological_processmitophagy
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
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0006914biological_processautophagy
A0006974biological_processDNA damage response
A0007249biological_processcanonical NF-kappaB signal transduction
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
A0018023biological_processpeptidyl-lysine trimethylation
A0019079biological_processviral genome replication
A0019674biological_processNAD+ metabolic process
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
A0035331biological_processnegative regulation of hippo signaling
A0035617biological_processstress granule disassembly
A0035800molecular_functiondeubiquitinase activator activity
A0035861cellular_componentsite of double-strand break
A0035869cellular_componentciliary transition zone
A0036064cellular_componentciliary basal body
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
A0043335biological_processprotein unfolding
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
A0097542cellular_componentciliary tip
A0098978cellular_componentglutamatergic synapse
A0106300biological_processprotein-DNA covalent cross-linking repair
A0120186biological_processnegative regulation of protein localization to chromatin
A0140036molecular_functionubiquitin-modified protein reader activity
A0140455biological_processcytoplasm protein quality control
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 Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11163219","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14988733","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine; by VCPKMT","evidences":[{"source":"PubMed","id":"22948820","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)","evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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