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2O3E

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006111biological_processregulation of gluconeogenesis
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0030163biological_processprotein catabolic process
A0042277molecular_functionpeptide binding
A0043171biological_processpeptide catabolic process
A0046872molecular_functionmetal ion binding
A0070012molecular_functionoligopeptidase activity
A1902809biological_processregulation of skeletal muscle fiber differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 679
ChainResidue
AHIS474
AHIS478
AGLU503
AHOH888

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TYFHEFGHVM
ChainResidueDetails
ATHR471-MET480

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9BYT8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i1i
ChainResidueDetails
ATYR613
AGLU503

site_idMCSA1
Number of Residues5
DetailsM-CSA 638
ChainResidueDetails
AHIS474
AGLU475
AHIS478
AGLU503proton shuttle (general acid/base)
ATYR613electrostatic stabiliser

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PDB entries from 2025-10-08

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