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5FAH

KALLIKREIN-7 IN COMPLEX WITH COMPOUND1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001533cellular_componentcornified envelope
A0002780biological_processantibacterial peptide biosynthetic process
A0004222molecular_functionmetalloendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0008544biological_processepidermis development
A0016787molecular_functionhydrolase activity
A0022617biological_processextracellular matrix disassembly
A0030141cellular_componentsecretory granule
A0051604biological_processprotein maturation
A0097209cellular_componentepidermal lamellar body
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ACT A 301
ChainResidue
ATRP29
AARG122
AVAL200
AGLY207
AHOH413
AHOH479

site_idAC2
Number of Residues18
Detailsbinding site for residue 5VT A 302
ChainResidue
AHIS57
ATHR96
APHE151
AASP154
AALA190
ACYS191
AASN192
AGLY193
AASP194
ASER195
ATRP215
AGLY216
ACYS220
AHOH481
AHOH529
AGLN39
AHIS41
ACYS42

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. NAcnGDSGGPLV
ChainResidueDetails
AASN189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"17909180","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Major binding site for inhibitory zinc or copper"}
ChainResidueDetails

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

247536

PDB entries from 2026-01-14

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