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5KNL

Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin

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
C0000209biological_processprotein polyubiquitination
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0061631molecular_functionubiquitin conjugating enzyme activity
C0061650molecular_functionubiquitin-like protein conjugating enzyme activity
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0004839molecular_functionubiquitin activating enzyme activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006511biological_processubiquitin-dependent protein catabolic process
D0006974biological_processDNA damage response
D0008641molecular_functionubiquitin-like modifier activating enzyme activity
D0016567biological_processprotein ubiquitination
D0016874molecular_functionligase activity
D0016887molecular_functionATP hydrolysis activity
D0036211biological_processprotein modification process
D0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000209biological_processprotein polyubiquitination
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0016567biological_processprotein ubiquitination
F0016740molecular_functiontransferase activity
F0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
F0061631molecular_functionubiquitin conjugating enzyme activity
F0061650molecular_functionubiquitin-like protein conjugating enzyme activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 1101
ChainResidue
AHIS29
AGLU30

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 1102
ChainResidue
APHE590
AARG601
AHIS604
CASP100
CARG110

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 1103
ChainResidue
AGLU603
ALYS843
CLYS101
AARG601
AILE602

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 1104
ChainResidue
AARG22
AASN471
AARG474

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 B 101
ChainResidue
AARG201
BARG29
BARG33

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 D 1101
ChainResidue
DGLY28
DHIS29
DGLU30

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 D 1102
ChainResidue
DARG610
DLYS850

site_idAC8
Number of Residues2
Detailsbinding site for residue SO4 D 1103
ChainResidue
DARG22
DARG474

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 F 201
ChainResidue
DPHE590
DARG601
DHIS604
FASP99
FARG110

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. WHPNVhpn.GeVCIsiL
ChainResidueDetails
CTRP79-LEU94

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 Residues12
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_FI8
Number of Residues160
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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