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6O21

Crystal Structure of Human KLK4 in Complex With Cleaved SFTI-FCQR(Asn14)[1,14] Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0022617biological_processextracellular matrix disassembly
A0030141cellular_componentsecretory granule
A0031214biological_processbiomineral tissue development
A0046872molecular_functionmetal ion binding
A0051604biological_processprotein maturation
A0097186biological_processamelogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SO4 A 301
ChainResidue
ATHR130
AALA132
ASER164
AGLU165
AHOH516
AHOH545
AHOH547
AHOH548

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG150
AMET151
AHOH414
AHOH444
AHOH482
AHOH505
ASER111

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 303
ChainResidue
ALYS217
AHOH462
AHOH535
BGLY1
BPHE2

site_idAC4
Number of Residues9
Detailsbinding site for residue MPD A 304
ChainResidue
AGLN187
ACYS220
AGLY220
ATHR235
AGLU236
AGLU239
AGLN243
AHOH429
AHOH514

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

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScnGDSGGPLI
ChainResidueDetails
AASP189-ILE200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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