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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6XOG

Structure of SUMO1-ML786519 adduct bound to SAE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004839molecular_functionubiquitin activating enzyme activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0008047molecular_functionenzyme activator activity
A0008641molecular_functionubiquitin-like modifier activating enzyme 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
A0036211biological_processprotein modification process
A0043008molecular_functionATP-dependent protein binding
A0044388molecular_functionsmall protein activating enzyme binding
A0046982molecular_functionprotein heterodimerization activity
A1903955biological_processpositive regulation of protein targeting to mitochondrion
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0016740molecular_functiontransferase activity
B0016925biological_processprotein sumoylation
B0019948molecular_functionSUMO activating enzyme activity
B0031510cellular_componentSUMO activating enzyme complex
B0032183molecular_functionSUMO binding
B0033235biological_processpositive regulation of protein sumoylation
B0044388molecular_functionsmall protein activating enzyme binding
B0044390molecular_functionubiquitin-like protein conjugating enzyme binding
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
C0001741cellular_componentXY body
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005643cellular_componentnuclear pore
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006281biological_processDNA repair
C0006355biological_processregulation of DNA-templated transcription
C0008076cellular_componentvoltage-gated potassium channel complex
C0008134molecular_functiontranscription factor binding
C0010621biological_processnegative regulation of transcription by transcription factor localization
C0015459molecular_functionpotassium channel regulator activity
C0016020cellular_componentmembrane
C0016604cellular_componentnuclear body
C0016605cellular_componentPML body
C0016607cellular_componentnuclear speck
C0016925biological_processprotein sumoylation
C0019899molecular_functionenzyme binding
C0030578biological_processPML body organization
C0031334biological_processpositive regulation of protein-containing complex assembly
C0031386molecular_functionprotein tag activity
C0031625molecular_functionubiquitin protein ligase binding
C0031647biological_processregulation of protein stability
C0031965cellular_componentnuclear membrane
C0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
C0032880biological_processregulation of protein localization
C0034605biological_processcellular response to heat
C0042308biological_processnegative regulation of protein import into nucleus
C0043392biological_processnegative regulation of DNA binding
C0043433biological_processnegative regulation of DNA-binding transcription factor activity
C0044388molecular_functionsmall protein activating enzyme binding
C0044389molecular_functionubiquitin-like protein ligase binding
C0045759biological_processnegative regulation of action potential
C0045892biological_processnegative regulation of DNA-templated transcription
C0050821biological_processprotein stabilization
C0060021biological_processroof of mouth development
C0071276biological_processcellular response to cadmium ion
C0086004biological_processregulation of cardiac muscle cell contraction
C0090204biological_processprotein localization to nuclear pore
C0097165cellular_componentnuclear stress granule
C0098978cellular_componentglutamatergic synapse
C0099523cellular_componentpresynaptic cytosol
C0099524cellular_componentpostsynaptic cytosol
C0141109molecular_functiontransporter activator activity
C1901017biological_processnegative regulation of potassium ion transmembrane transporter activity
C1902260biological_processnegative regulation of delayed rectifier potassium channel activity
C1903169biological_processregulation of calcium ion transmembrane transport
C1990381molecular_functionubiquitin-specific protease binding
Functional Information from PROSITE/UniProt
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 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_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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_FI8
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_FI9
Number of Residues7
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_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)"}
ChainResidueDetails
site_idSWS_FT_FI11
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_FI12
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsRegion: {"description":"(Microbial infection) Interaction with Tula hantavirus","evidences":[{"source":"PubMed","id":"12606074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Interaction with PIAS2"}
ChainResidueDetails
site_idSWS_FT_FI15
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_FI16
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
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

238895

PDB entries from 2025-07-16

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