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6O83

S. pombe ubiquitin E1~ubiquitin-AMP tetrahedral intermediate mimic

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004839molecular_functionubiquitin activating enzyme activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0006974biological_processDNA damage response
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
A0016567biological_processprotein ubiquitination
A0016874molecular_functionligase activity
A0016887molecular_functionATP hydrolysis activity
A0036211biological_processprotein modification process
A0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0004839molecular_functionubiquitin activating enzyme activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0006974biological_processDNA damage response
C0008641molecular_functionubiquitin-like modifier activating enzyme activity
C0016567biological_processprotein ubiquitination
C0016874molecular_functionligase activity
C0016887molecular_functionATP hydrolysis activity
C0036211biological_processprotein modification process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 1101
ChainResidue
AHIS305
AGLU320
AASP715
AHIS717

site_idAC2
Number of Residues4
Detailsbinding site for residue TRS A 1102
ChainResidue
AGLU553
AARG919
AASN921
ACYS1009

site_idAC3
Number of Residues2
Detailsbinding site for residue MPD A 1103
ChainResidue
ATYR378
ATHR175

site_idAC4
Number of Residues4
Detailsbinding site for residue MPD A 1104
ChainResidue
AGLN136
ASER161
APHE295
ATYR385

site_idAC5
Number of Residues3
Detailsbinding site for residue MPD A 1105
ChainResidue
AGLU658
AGLU665
AMET668

site_idAC6
Number of Residues4
Detailsbinding site for residue MPD A 1106
ChainResidue
AARG547
AVAL990
AGLU992
APHE1007

site_idAC7
Number of Residues3
Detailsbinding site for residue MPD A 1107
ChainResidue
AILE716
AHIS717
AGLU748

site_idAC8
Number of Residues13
Detailsbinding site for residue VMX A 1108
ChainResidue
AALA437
AILE438
AASP463
AMET464
AASP465
ALYS487
AVAL513
AALA535
AASP537
AASN538
ATHR561
ACYS593
BGLY75

site_idAC9
Number of Residues4
Detailsbinding site for residue CA C 1101
ChainResidue
CHIS305
CGLU320
CASP715
CHIS717

site_idAD1
Number of Residues6
Detailsbinding site for residue TRS C 1102
ChainResidue
CGLU553
CARG919
CASN921
CHIS988
CCYS1009
CLYS1011

site_idAD2
Number of Residues3
Detailsbinding site for residue MPD C 1103
ChainResidue
CGLU658
CGLU665
CLEU672

site_idAD3
Number of Residues5
Detailsbinding site for residue MPD C 1104
ChainResidue
CASP68
CPRO69
CGLN70
CGLU130
CTHR131

site_idAD4
Number of Residues2
Detailsbinding site for residue MPD C 1105
ChainResidue
CGLU577
CSER582

site_idAD5
Number of Residues3
Detailsbinding site for residue MPD C 1106
ChainResidue
CILE716
CPHE722
CGLU748

site_idAD6
Number of Residues5
Detailsbinding site for residue MPD C 1107
ChainResidue
CLEU133
CGLN136
CSER161
CPHE295
CTYR385

site_idAD7
Number of Residues3
Detailsbinding site for residue MPD C 1108
ChainResidue
CVAL990
CGLU992
CPHE1007

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KskIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52

site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PICTLKnFP
ChainResidueDetails
APRO591-PRO599

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10132","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23416107","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4II2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4II3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22515","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23416107","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4II2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P22515","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P22515","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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