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5F6E

Crystal Structure of human Ubc9 (K48A/K49A/E54A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000795cellular_componentsynaptonemal complex
A0001221molecular_functiontranscription coregulator binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0007059biological_processchromosome segregation
A0007084biological_processmitotic nuclear membrane reassembly
A0008134molecular_functiontranscription factor binding
A0016605cellular_componentPML body
A0016740molecular_functiontransferase activity
A0016925biological_processprotein sumoylation
A0019787molecular_functionubiquitin-like protein transferase activity
A0019789molecular_functionSUMO transferase activity
A0019899molecular_functionenzyme binding
A0030335biological_processpositive regulation of cell migration
A0032446biological_processprotein modification by small protein conjugation
A0036211biological_processprotein modification process
A0044388molecular_functionsmall protein activating enzyme binding
A0045892biological_processnegative regulation of DNA-templated transcription
A0048471cellular_componentperinuclear region of cytoplasm
A0051168biological_processnuclear export
A0051301biological_processcell division
A0061656molecular_functionSUMO conjugating enzyme activity
A0071535molecular_functionRING-like zinc finger domain binding
A0106068cellular_componentSUMO ligase complex
A1903755biological_processpositive regulation of SUMO transferase activity
A1990234cellular_componenttransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 201
ChainResidue
AVAL92
ACYS93
ALEU94
ALEU97
AGLU98
AHOH304

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL
ChainResidueDetails
APHE82-LEU97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate
ChainResidueDetails
ACYS93

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Interaction with RANBP2
ChainResidueDetails
AILE4
AVAL25
ALEU57

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Substrate binding
ChainResidueDetails
AASP100

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS65

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:22509284, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER71

site_idSWS_FT_FI7
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
ALYS18

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS101

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
AALA48

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
AALA49

226707

PDB entries from 2024-10-30

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