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5Y2Z

Crystal structure of human LGI1 EPTP-ADAM22 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
C0004222molecular_functionmetalloendopeptidase activity
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
E0008237molecular_functionmetallopeptidase activity
G0004222molecular_functionmetalloendopeptidase activity
G0006508biological_processproteolysis
G0008237molecular_functionmetallopeptidase activity
I0004222molecular_functionmetalloendopeptidase activity
I0006508biological_processproteolysis
I0008237molecular_functionmetallopeptidase activity
K0004222molecular_functionmetalloendopeptidase activity
K0006508biological_processproteolysis
K0008237molecular_functionmetallopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CvCnrHwiGSdC
ChainResidueDetails
ACYS700-CYS711

site_idPS00427
Number of Residues20
DetailsDISINTEGRIN_1 Disintegrins signature. CsdGlCCk.KCkFqpmgtvCR
ChainResidueDetails
ACYS485-ARG504

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1194
DetailsDomain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues522
DetailsDomain: {"description":"Disintegrin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00068","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues222
DetailsDomain: {"description":"EGF-like"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues17
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19692335","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues252
DetailsRepeat: {"description":"EAR 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues252
DetailsRepeat: {"description":"EAR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues282
DetailsRepeat: {"description":"EAR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues294
DetailsRepeat: {"description":"EAR 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues258
DetailsRepeat: {"description":"EAR 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues252
DetailsRepeat: {"description":"EAR 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues42
DetailsRepeat: {"description":"EAR 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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