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3CNQ

Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM

Functional Information from GO Data
ChainGOidnamespacecontents
S0004252molecular_functionserine-type endopeptidase activity
S0006508biological_processproteolysis
S0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN S 278
ChainResidue
SALA169
STYR171

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN S 279
ChainResidue
PGLU27
SHIS238

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN S 280
ChainResidue
SHIS39
SPRO40
SASP41

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN S 281
ChainResidue
SHIS17

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN S 282
ChainResidue
SASP259
PGLU32

Functional Information from PROSITE/UniProt
site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVLA
ChainResidueDetails
SHIS64-ALA74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818
ChainResidueDetails
SALA32
SHIS64
SALA230

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
SLYS2
SASP41
SVAL84
SPRO86
SALA88
SLEU90
SGLY178
SVAL180
SSER183

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 723
ChainResidueDetails
SALA32electrostatic interaction, electrostatic stabiliser
SHIS64proton acceptor, proton donor
STHR164electrostatic interaction, electrostatic stabiliser
SALA230nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-07-10

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