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4XXB

Crystal structure of human MDM2-RPL11

Functional Information from GO Data
ChainGOidnamespacecontents
A0000027biological_processribosomal large subunit assembly
A0002181biological_processcytoplasmic translation
A0003723molecular_functionRNA binding
A0003735molecular_functionstructural constituent of ribosome
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005840cellular_componentribosome
A0006364biological_processrRNA processing
A0006412biological_processtranslation
A0006605biological_processprotein targeting
A0006941biological_processstriated muscle contraction
A0007283biological_processspermatogenesis
A0008097molecular_function5S rRNA binding
A0016020cellular_componentmembrane
A0019843molecular_functionrRNA binding
A0022625cellular_componentcytosolic large ribosomal subunit
A0022626cellular_componentcytosolic ribosome
A0031625molecular_functionubiquitin protein ligase binding
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032991cellular_componentprotein-containing complex
A0034504biological_processprotein localization to nucleus
A0042273biological_processribosomal large subunit biogenesis
A0070062cellular_componentextracellular exosome
A1901740biological_processnegative regulation of myoblast fusion
A1901796biological_processregulation of signal transduction by p53 class mediator
A1901798biological_processpositive regulation of signal transduction by p53 class mediator
A1990904cellular_componentribonucleoprotein complex
A1990948molecular_functionubiquitin ligase inhibitor activity
A2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
B0005634cellular_componentnucleus
B0043066biological_processnegative regulation of apoptotic process
B0051726biological_processregulation of cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue IMD A 201
ChainResidue
ACYS25
AILE68
AALA69
AZN203
BPRO316
BHIS318
BASN320

site_idAC2
Number of Residues5
Detailsbinding site for residue BME A 202
ChainResidue
BASP294
BPRO314
BLEU315
ACYS21
ATYR131

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 203
ChainResidue
ACYS25
AIMD201
AHOH322
BHIS318

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BCYS305
BCYS308
BCYS319
BCYS322

Functional Information from PROSITE/UniProt
site_idPS00358
Number of Residues17
DetailsRIBOSOMAL_L5 Ribosomal protein L5 signature. LeqLTGQtpVfSkARyT
ChainResidueDetails
ALEU40-THR56

site_idPS01358
Number of Residues20
DetailsZF_RANBP2_1 Zinc finger RanBP2-type signature. WkCts..CnemNpplpshCnrC
ChainResidueDetails
BTRP303-CYS322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues29
DetailsZinc finger: {"description":"RanBP2-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00322","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37291423","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BGU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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