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2O36

Crystal structure of engineered thimet oligopeptidase with neurolysin specificity in neurotensin cleavage site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005758cellular_componentmitochondrial intermembrane space
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0008237molecular_functionmetallopeptidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 690
ChainResidue
AHIS473
AHIS477
AGLU502
AHOH1161

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TYFHEFGHVM
ChainResidueDetails
ATHR470-MET479

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:17251185
ChainResidueDetails
AGLU474

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17251185
ChainResidueDetails
AHIS473
AHIS477
AHIS480

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER16

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8C1A5
ChainResidueDetails
ASER172

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS257
ALYS538

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8C1A5
ChainResidueDetails
ATYR278

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i1i
ChainResidueDetails
ATYR612
AGLU502

221716

PDB entries from 2024-06-26

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