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5F8X

The crystal structure of human plasma kallikrein in complex with its peptide inhibitor pkalin-3

Replaces:  4ZJ6
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 301
ChainResidue
ALEU60
APRO60
AMET235
AHOH427
AHOH447

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
AGLY69
ATHR115
AGLN118
AHOH439

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLU26
ATRP137
ALYS157
AHOH494

site_idAC4
Number of Residues9
Detailsbinding site for residue SO4 A 304
ChainResidue
ATRP24
AGLY25
ATRP27
AGLY69
AILE70
ALEU71
APHE117
ALEU155
AHOH431

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 305
ChainResidue
ALEU37
ATHR38
AALA38
AARG39
ALYS119
ALYS185

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 A 306
ChainResidue
ATRP24
APHE117
AASN159
APRO161
ATYR184
AHOH549

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 A 307
ChainResidue
AGLN34
AGLN38
ALEU73
AILE76

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 A 308
ChainResidue
ATYR184
AGLY186
ALYS186
AHOH532

site_idAC9
Number of Residues9
Detailsbinding site for residue MRZ B 100
ChainResidue
AASP189
AALA190
ATHR213
ATRP215
AGLY219
AGLY226
AHOH499
BPHE5
BALA6

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
AASN21
AASN113

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
AASN72

226707

PDB entries from 2024-10-30

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