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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3RZW

Crystal Structure of the Monobody ySMB-9 bound to human SUMO1

Functional Information from GO Data
ChainGOidnamespacecontents
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_processobsolete negative 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
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
D0006355biological_processregulation of DNA-templated transcription
D0008076cellular_componentvoltage-gated potassium channel complex
D0008134molecular_functiontranscription factor binding
D0010621biological_processobsolete negative regulation of transcription by transcription factor localization
D0015459molecular_functionpotassium channel regulator activity
D0016020cellular_componentmembrane
D0016604cellular_componentnuclear body
D0016605cellular_componentPML body
D0016607cellular_componentnuclear speck
D0016925biological_processprotein sumoylation
D0019899molecular_functionenzyme binding
D0030578biological_processPML body organization
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
D0032880biological_processregulation of protein localization
D0034605biological_processcellular response to heat
D0042308biological_processnegative regulation of protein import into nucleus
D0043392biological_processnegative regulation of DNA binding
D0043433biological_processnegative regulation of DNA-binding transcription factor activity
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
D0071276biological_processcellular response to cadmium ion
D0086004biological_processregulation of cardiac muscle cell contraction
D0090204biological_processprotein localization to nuclear pore
D0097165cellular_componentnuclear stress granule
D0098978cellular_componentglutamatergic synapse
D0099523cellular_componentpresynaptic cytosol
D0099524cellular_componentpostsynaptic cytosol
D0141109molecular_functiontransporter activator activity
D1901017biological_processnegative regulation of potassium ion transmembrane transporter activity
D1902260biological_processnegative regulation of delayed rectifier potassium channel activity
D1903169biological_processregulation of calcium ion transmembrane transport
D1990381molecular_functionubiquitin-specific protease binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 91
ChainResidue
BSER17
BLEU18
site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 92
ChainResidue
BTYR36
BTHR58
BSER60
DGLN92
DGLN94
Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP
ChainResidueDetails
AGLY37-PRO44
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsRegion: {"description":"(Microbial infection) Interaction with Tula hantavirus","evidences":[{"source":"PubMed","id":"12606074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Interaction with PIAS2"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
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_FI5
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)"}
ChainResidueDetails
site_idSWS_FT_FI6
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_FI7
Number of Residues77
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
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

240971

PDB entries from 2025-08-27

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