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1I1I

NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE

Functional Information from GO Data
ChainGOidnamespacecontents
P0004222molecular_functionmetalloendopeptidase activity
P0005758cellular_componentmitochondrial intermembrane space
P0005829cellular_componentcytosol
P0006508biological_processproteolysis
P0008233molecular_functionpeptidase activity
P0008237molecular_functionmetallopeptidase activity
P0030163biological_processprotein catabolic process
P0043171biological_processpeptide catabolic process
P0070012molecular_functionoligopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN P 701
ChainResidue
PHIS474
PHIS478
PGLU503
PSER506
PHOH703

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN P 702
ChainResidue
PHIS125
PHIS160
PGLU164
PHOH817

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TYFHEFGHVM
ChainResidueDetails
PTHR471-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
Detailsa catalytic site defined by CSA, PubMed 11248043
ChainResidueDetails
PTYR613
PGLU503

site_idMCSA1
Number of Residues5
DetailsM-CSA 638
ChainResidueDetails

251422

PDB entries from 2026-04-01

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