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1O3P

Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT B 1
ChainResidue
BCIT2
BTYR67
BASN76
BGLU80
BLYS82
BSER164
BHIS165
BARG166
BHOH498

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT B 2
ChainResidue
BCIT1
BARG36
BLYS82
BLYS110
BHIS165
BARG230
BHOH276
BHOH382

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 655 B 251
ChainResidue
BHIS57
BCYS58
BGLN185
BSER190
BCYS191
BGLN192
BSER195
BVAL213
BTRP215
BGLY219
BHOH419
BHOH464
BHOH521
BHOH534

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. ISATHC
ChainResidueDetails
BILE53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV
ChainResidueDetails
BASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS57
BASP102
BSER195

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9151681
ChainResidueDetails
BSER146

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
BALA145

221051

PDB entries from 2024-06-12

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