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2ANY

Expression, Crystallization and the Three-dimensional Structure of the Catalytic Domain of Human Plasma Kallikrein: Implications for Structure-Based Design of Protease Inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 2
ChainResidue
APO43
ATHR77
ALYS78
ALYS202
AHOH304
AHOH549
AHOH632
AHOH640

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 3
ChainResidue
AASP173
ALYS202
AHIS203
AASN204
AGLY205
AHOH362
AHOH549
AHOH640
APO42

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 4
ChainResidue
AHIS91
AGLN92
AARG179
ATRP237
AHOH635

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEN A 1
ChainResidue
AASP189
AALA190
ASER195
ASER214
ATRP215
AGLY219
AGLY226
AHOH576

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLV
ChainResidueDetails
AASP189-VAL200

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

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732
ChainResidueDetails
AGLU21
AGLU113

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732
ChainResidueDetails
AGLU72

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PDB entries from 2024-06-12

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