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5MNJ

Structure of MDM2-MDMX-UbcH5B-ubiquitin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0032991cellular_componentprotein-containing complex
A0036211biological_processprotein modification process
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070062cellular_componentextracellular exosome
A0070936biological_processprotein K48-linked ubiquitination
C0042802molecular_functionidentical protein binding
C0061630molecular_functionubiquitin protein ligase activity
D0005634cellular_componentnucleus
D0043066biological_processnegative regulation of apoptotic process
D0051726biological_processregulation of cell cycle
E0000166molecular_functionnucleotide binding
E0000209biological_processprotein polyubiquitination
E0004842molecular_functionubiquitin-protein transferase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005829cellular_componentcytosol
E0006511biological_processubiquitin-dependent protein catabolic process
E0016567biological_processprotein ubiquitination
E0016740molecular_functiontransferase activity
E0032991cellular_componentprotein-containing complex
E0036211biological_processprotein modification process
E0051865biological_processprotein autoubiquitination
E0061630molecular_functionubiquitin protein ligase activity
E0061631molecular_functionubiquitin conjugating enzyme activity
E0070062cellular_componentextracellular exosome
E0070936biological_processprotein K48-linked ubiquitination
G0042802molecular_functionidentical protein binding
G0061630molecular_functionubiquitin protein ligase activity
H0005634cellular_componentnucleus
H0043066biological_processnegative regulation of apoptotic process
H0051726biological_processregulation of cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN C 501
ChainResidue
CCYS438
CCYS441
CCYS461
CCYS464

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN C 502
ChainResidue
CHIS452
CHIS457
CCYS475
CCYS478

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN D 501
ChainResidue
DCYS440
DCYS460
DCYS463
DCYS437

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN D 502
ChainResidue
DHIS451
DHIS456
DCYS474
DCYS477

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 D 503
ChainResidue
DALA472
DSER473
DLYS478
EARG139
HALA472
HSER473
HLYS478

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN G 501
ChainResidue
GCYS438
GCYS441
GCYS461
GCYS464

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN G 502
ChainResidue
GHIS452
GHIS457
GCYS475
GCYS478

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN H 501
ChainResidue
HHIS451
HHIS456
HCYS474
HCYS477

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN H 502
ChainResidue
HCYS437
HCYS440
HCYS460
HCYS463

site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 H 503
ChainResidue
DLYS442
DARG443
DARG466
HLYS442
HARG443
HARG466

site_idAD2
Number of Residues10
Detailsbinding site for Di-peptide GLY F 76 and LYS E 85
ChainResidue
EHIS75
EASN77
EILE78
EILE84
ELEU86
EASP117
ELEU119
EVAL120
ETYR134
FGLY75

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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

site_idSWS_FT_FI2
Number of Residues75
DetailsDomain: {"description":"Ubiquitin-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues164
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsMotif: {"description":"Nucleolar localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by ATM","evidences":[{"source":"PubMed","id":"19816404","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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