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4GI3

Crystal structure of Greglin in complex with subtilisin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
C0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH
ChainResidueDetails
AVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA
ChainResidueDetails
AHIS64-ALA74

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG
ChainResidueDetails
AGLY219-GLY229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16839309, ECO:0000269|PubMed:23075397
ChainResidueDetails
CSER8

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16839309
ChainResidueDetails
CSER11
CSER15

222415

PDB entries from 2024-07-10

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