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1SHY

The Crystal Structure of HGF beta-chain in Complex with the Sema Domain of the Met Receptor.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0017154molecular_functionsemaphorin receptor activity
B0071526biological_processsemaphorin-plexin signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues226
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000024","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000025","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19196183","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
AGLY674
ATYR673

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
AGLY671
ATYR673

246704

PDB entries from 2025-12-24

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