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CRYSTAL STRUCTURE OF WILD-TYPE ALPHA-LYTIC PROTEASE AT 1.6 A, PH 5.14

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
AARG25
AHOH382
AHOH429
AARG78
AGLN190
ATYR191
AHOH230
AHOH231
AHOH232
AHOH380
AHOH381

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
AALA1
AASN2
AARG183
APRO186
AHOH207
AHOH273
AHOH342
AHOH343
AHOH398
AHOH399

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
AHIS36
AARG89
AARG140
AGLY141
ASER143
AGOL201
AHOH361
AHOH362
AHOH363

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AHIS36
AARG89
ATYR123
AGLU125
ASER159
AGLY160
ASO4204

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC
ChainResidueDetails
AVAL32-CYS37

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. CMgrGDSGGSWI
ChainResidueDetails
ACYS137-ILE148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
AHIS36
AASP63
ASER143

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
ASER143
AGLY141
AASP63
AHIS36
ASER159

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
ASER143
AGLY141
AASP63
AHIS36

site_idMCSA1
Number of Residues5
DetailsM-CSA 609
ChainResidueDetails
AHIS36proton acceptor, proton donor
AASP63electrostatic stabiliser
AGLY141electrostatic stabiliser
ASER143electrostatic stabiliser
ASER159electrostatic stabiliser

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PDB entries from 2024-08-28

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