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6ZHT

Uba1-Ubc13 disulfide mediated complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0000209biological_processprotein polyubiquitination
B0000329cellular_componentfungal-type vacuole membrane
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006301biological_processpostreplication repair
B0010994biological_processfree ubiquitin chain polymerization
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0031371cellular_componentubiquitin conjugating enzyme complex
B0044395biological_processprotein targeting to vacuolar membrane
B0061631molecular_functionubiquitin conjugating enzyme activity
B0070534biological_processprotein K63-linked ubiquitination
C0000166molecular_functionnucleotide binding
C0004839molecular_functionubiquitin activating enzyme activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006511biological_processubiquitin-dependent protein catabolic process
C0006974biological_processDNA damage response
C0008641molecular_functionubiquitin-like modifier activating enzyme activity
C0016567biological_processprotein ubiquitination
C0016874molecular_functionligase activity
C0036211biological_processprotein modification process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL C 1101
ChainResidue
CSER153
CGLU155
CASN162
CPHE296
CGLN297
CHOH1204
CHOH1213

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL C 1102
ChainResidue
CHOH1230
CGLU525
CTYR959

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL C 1103
ChainResidue
CGLU534
CPHE558
CTYR559
CARG930
CHOH1282

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL C 1104
ChainResidue
CASN900
CLEU903

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL C 1105
ChainResidue
CARG554
CVAL557
CILE1002
CGLU1004
CPHE1019

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL C 1106
ChainResidue
CLYS45
CGLU69
CARG91
CTHR131
CHOH1284

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL C 1107
ChainResidue
CLYS430
CGLY461
CSER462

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL C 1109
ChainResidue
CALA614
CLYS617
CSER618
CGLN621
CHOH1272

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL C 1110
ChainResidue
CASP932
CLYS934
CLYS934
CHIS1023

site_idAD1
Number of Residues8
Detailsbinding site for residue GOL C 1111
ChainResidue
CASP470
CASN471
CASP518
CLYS519
CVAL520
CLEU543
CALA548
CHOH1412

site_idAD2
Number of Residues4
Detailsbinding site for residue CL C 1112
ChainResidue
CGLN372
CLEU375
CSER379
CPHE382

site_idAD3
Number of Residues2
Detailsbinding site for residue CL C 1113
ChainResidue
CLYS229
CLYS229

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL B 201
ChainResidue
BILE86
BCYS87
BLEU88
BLEU91
BLYS92
CPRO598
CLEU599

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNIdrl.GrICLdvL
ChainResidueDetails
BTYR76-LEU91

site_idPS00536
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KACSGKFtP
ChainResidueDetails
CLYS376-PRO384

site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PLCTLRsFP
ChainResidueDetails
CPRO598-PRO606

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues137
DetailsRepeat: {"description":"1-1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues154
DetailsRepeat: {"description":"1-2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues552
DetailsRegion: {"description":"2 approximate repeats"}
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":"24816100","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35970836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24816100","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7ZH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35970836","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ZH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues5
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues146
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 307
ChainResidueDetails

site_idMCSA2
Number of Residues3
DetailsM-CSA 939
ChainResidueDetails

239492

PDB entries from 2025-07-30

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