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6SQO

Crystal structure of human MDM2 RING domain homodimer bound to UbcH5B-Ub

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0042802molecular_functionidentical protein binding
A0043066biological_processnegative regulation of apoptotic process
A0051726biological_processregulation of cell cycle
A0061630molecular_functionubiquitin protein ligase activity
B0000166molecular_functionnucleotide binding
B0000209biological_processprotein polyubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0032991cellular_componentprotein-containing complex
B0036211biological_processprotein modification process
B0051865biological_processprotein autoubiquitination
B0061630molecular_functionubiquitin protein ligase activity
B0061631molecular_functionubiquitin conjugating enzyme activity
B0070062cellular_componentextracellular exosome
B0070936biological_processprotein K48-linked ubiquitination
D0005634cellular_componentnucleus
D0042802molecular_functionidentical protein binding
D0043066biological_processnegative regulation of apoptotic process
D0051726biological_processregulation of cell cycle
D0061630molecular_functionubiquitin protein ligase activity
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
ACYS438
ACYS441
ACYS461
ACYS464

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
AHIS452
AHIS457
ACYS475
ACYS478

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 503
ChainResidue
AILE485

site_idAC4
Number of Residues4
Detailsbinding site for residue CL B 201
ChainResidue
AHOH622
BALA2
BLEU3
BLYS4

site_idAC5
Number of Residues2
Detailsbinding site for residue NO3 B 202
ChainResidue
BARG136
BGLU140

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN D 501
ChainResidue
DCYS438
DCYS441
DCYS461
DCYS464

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN D 502
ChainResidue
DHIS452
DHIS457
DCYS475
DCYS478

site_idAC8
Number of Residues1
Detailsbinding site for residue CL D 503
ChainResidue
DILE485

site_idAC9
Number of Residues4
Detailsbinding site for residue CL E 201
ChainResidue
EALA2
ELEU3
ELYS4
EHOH422

site_idAD1
Number of Residues5
Detailsbinding site for residue NO3 E 202
ChainResidue
ELYS85
EARG90
ELYS133
EARG136
EHOH322

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues82
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsMotif: {"description":"Nucleolar localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
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_FI4
Number of Residues150
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"ADP-ribosylglycine","evidences":[{"source":"PubMed","id":"28525742","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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