Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5TJX

Structure of human plasma kallikrein

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue GBT A 701
ChainResidue
AHIS434
ASER578
ATHR596
ASER597
ATRP598
AGLY599
AGLY601
ACYS602
APO4702
AHOH846
AHOH896
ASER478
AHOH897
AHOH947
AGLU479
AGLY480
ATYR555
AMET561
AASP572
AALA573
ACYS574

site_idAC2
Number of Residues9
Detailsbinding site for residue PO4 A 702
ChainResidue
ALEU418
AHIS434
ALYS575
AGLY576
ASER578
AGBT701
AHOH811
AHOH816
AHOH823

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 703
ChainResidue
AHIS472
AGLN473
AARG560
AHOH955
AHOH957

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU430-CYS435

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLV
ChainResidueDetails
AASP572-VAL583

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS434
AASP483
ASER578

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
AGLU396
AGLU494

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
AGLU453

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon