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10MT

C2 symmetry expanded and subtracted 20S Proteasome, Blm10, Fub1 Complex Halfmer

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00388
Number of Residues23
DetailsPROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdrgvStFSPeGRlfQVEYSleA
ChainResidueDetails
ETYR8-ALA30
ATYR12-ALA34
GTYR7-ALA29
BTYR5-ALA27
CTYR4-ALA26
FTYR6-ALA28

site_idPS00854
Number of Residues47
DetailsPROTEASOME_BETA_1 Proteasome beta-type subunits signature. VAMtGkdCVAIACDlrlgsqslgvsnkfe.Kifhyghvflgit.GlaTD
ChainResidueDetails
JVAL13-ASP59
KLEU5-ASP52
HMET23-ASP70
MLEU32-ASP79
IVAL33-ASP80
NILE45-ASP92
LLEU79-ASP126
CVAL34-ASP81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9087403","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues39
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues35
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"HEAT 3"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues38
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues84
DetailsRegion: {"description":"Bromodomain-like (BRDL)"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsMotif: {"description":"YYX motif"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 177
ChainResidueDetails
FLYS30covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
FLEU46activator, steric locator
FALA48activator
FLYS62activator, electrostatic stabiliser
FGLY76electrostatic stabiliser
FGLY158activator, electrostatic stabiliser
FGLU195activator, steric locator
FSER198activator, electrostatic stabiliser

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PDB entries from 2026-07-22

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