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2LPR

STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AALA15
AASN15
AARG230
APRO233
AHOH270
AHOH281
AHOH371

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR CHAIN P OF METHOXYSUCCINYL-ALA-ALA-PRO-VALINE BORONIC ACID INHIBITOR
ChainResidue
ATYR171
AGLY192
AGLY193
AASP194
ASER195
AMET213
ASER214
AGLY215
AGLY216
AVAL217
PHOH89
PHOH102
AHIS57
AARG125

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. CAgrGDSGGSWI
ChainResidueDetails
ACYS191-ILE200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
AHIS57
AASP102
ASER195

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 3122831, 12475199
ChainResidueDetails
AASP102
AGLY193
AHIS57

site_idMCSA1
Number of Residues5
DetailsM-CSA 609
ChainResidueDetails
AHIS57proton acceptor, proton donor
AASP102electrostatic stabiliser
AGLY193electrostatic stabiliser
ASER195electrostatic stabiliser
ASER214electrostatic stabiliser

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PDB entries from 2024-07-17

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