Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9DRJ

Cryo-EM structure of a SUMO E1-E2-SUMO1 complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004839molecular_functionubiquitin activating enzyme activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008047molecular_functionenzyme activator activity
A0016567biological_processprotein ubiquitination
A0016874molecular_functionligase activity
A0016925biological_processprotein sumoylation
A0019948molecular_functionSUMO activating enzyme activity
A0031510cellular_componentSUMO activating enzyme complex
A0033235biological_processpositive regulation of protein sumoylation
A0043008molecular_functionATP-dependent protein binding
A0044388molecular_functionsmall protein activating enzyme binding
A0046982molecular_functionprotein heterodimerization activity
A1903955biological_processpositive regulation of protein targeting to mitochondrion
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000166molecular_functionnucleotide binding
C0000795cellular_componentsynaptonemal complex
C0001221molecular_functiontranscription coregulator binding
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005635cellular_componentnuclear envelope
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0007059biological_processchromosome segregation
C0007084biological_processmitotic nuclear membrane reassembly
C0008134molecular_functiontranscription factor binding
C0016604cellular_componentnuclear body
C0016605cellular_componentPML body
C0016740molecular_functiontransferase activity
C0016925biological_processprotein sumoylation
C0019789molecular_functionSUMO transferase activity
C0019899molecular_functionenzyme binding
C0030335biological_processpositive regulation of cell migration
C0036211biological_processprotein modification process
C0043398molecular_functionHLH domain binding
C0044388molecular_functionsmall protein activating enzyme binding
C0045892biological_processnegative regulation of DNA-templated transcription
C0048471cellular_componentperinuclear region of cytoplasm
C0050804biological_processmodulation of chemical synaptic transmission
C0051168biological_processnuclear export
C0051170biological_processimport into nucleus
C0051301biological_processcell division
C0061656molecular_functionSUMO conjugating enzyme activity
C0071535molecular_functionRING-like zinc finger domain binding
C0098685cellular_componentSchaffer collateral - CA1 synapse
C0098978cellular_componentglutamatergic synapse
C0099523cellular_componentpresynaptic cytosol
C0099524cellular_componentpostsynaptic cytosol
C0106068cellular_componentSUMO ligase complex
C1990234cellular_componenttransferase complex
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0001741cellular_componentXY body
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005643cellular_componentnuclear pore
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006281biological_processDNA repair
D0015459molecular_functionpotassium channel regulator activity
D0016604cellular_componentnuclear body
D0016605cellular_componentPML body
D0016607cellular_componentnuclear speck
D0016925biological_processprotein sumoylation
D0019899molecular_functionenzyme binding
D0031334biological_processpositive regulation of protein-containing complex assembly
D0031386molecular_functionprotein tag activity
D0031625molecular_functionubiquitin protein ligase binding
D0031647biological_processregulation of protein stability
D0031965cellular_componentnuclear membrane
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0034605biological_processcellular response to heat
D0042308biological_processnegative regulation of protein import into nucleus
D0044388molecular_functionsmall protein activating enzyme binding
D0044389molecular_functionubiquitin-like protein ligase binding
D0045759biological_processnegative regulation of action potential
D0045892biological_processnegative regulation of DNA-templated transcription
D0050821biological_processprotein stabilization
D0060021biological_processroof of mouth development
D0060633biological_processnegative regulation of transcription initiation by RNA polymerase II
D0071276biological_processcellular response to cadmium ion
D0086004biological_processregulation of cardiac muscle cell contraction
D0097165cellular_componentnuclear stress granule
D0098978cellular_componentglutamatergic synapse
D0099523cellular_componentpresynaptic cytosol
D0099524cellular_componentpostsynaptic cytosol
D0141109molecular_functiontransporter activator activity
D1903169biological_processregulation of calcium ion transmembrane transport
D1990381molecular_functionubiquitin-specific protease binding
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL
ChainResidueDetails
CPHE82-LEU97
site_idPS00536
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KILSGKIdQ
ChainResidueDetails
BLYS404-GLN412
site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PGCTIRnTP
ChainResidueDetails
BPRO171-PRO179
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues29
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues9
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10132","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20164921","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues9
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues153
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues5
DetailsRegion: {"description":"Interaction with SUMO1"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsSite: {"description":"Interaction with RANBP2"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsSite: {"description":"Substrate binding"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"22509284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues3
DetailsRegion: {"description":"(Microbial infection) Interaction with Tula hantavirus","evidences":[{"source":"PubMed","id":"12606074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsSite: {"description":"Interaction with PIAS2"}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)","evidences":[{"source":"PubMed","id":"27068747","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)"}
ChainResidueDetails

247035

PDB entries from 2026-01-07

PDB statisticsPDBj update infoContact PDBjnumon