1S4B

Crystal structure of human thimet oligopeptidase.

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0000209	biological_process	protein polyubiquitination
P	0004222	molecular_function	metalloendopeptidase activity
P	0005515	molecular_function	protein binding
P	0005737	cellular_component	cytoplasm
P	0005758	cellular_component	mitochondrial intermembrane space
P	0005829	cellular_component	cytosol
P	0006508	biological_process	proteolysis
P	0008233	molecular_function	peptidase activity
P	0008237	molecular_function	metallopeptidase activity
P	0016787	molecular_function	hydrolase activity
P	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TYFHEFGHVM

Chain	Residue	Details
P	THR470-MET479

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"17251185","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17251185","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8C1A5","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8C1A5","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1i1i