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1S4B

Crystal structure of human thimet oligopeptidase.

Functional Information from GO Data
ChainGOidnamespacecontents
P0000209biological_processprotein polyubiquitination
P0004222molecular_functionmetalloendopeptidase activity
P0005515molecular_functionprotein binding
P0005737cellular_componentcytoplasm
P0005758cellular_componentmitochondrial intermembrane space
P0005829cellular_componentcytosol
P0006508biological_processproteolysis
P0006518biological_processpeptide metabolic process
P0008233molecular_functionpeptidase activity
P0008237molecular_functionmetallopeptidase activity
P0016787molecular_functionhydrolase activity
P0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN P 1
ChainResidue
PHIS473
PHIS477
PGLU502
PHOH1163

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TYFHEFGHVM
ChainResidueDetails
PTHR470-MET479

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:17251185
ChainResidueDetails
PPHE475

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17251185
ChainResidueDetails
PGLU474
PVAL478
PGLN481

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
PPRO17

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8C1A5
ChainResidueDetails
PLEU173

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
PGLU258
PLEU539

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8C1A5
ChainResidueDetails
PVAL279

218853

PDB entries from 2024-04-24

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