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4KEL

Atomic resolution crystal structure of Kallikrein-Related Peptidase 4 complexed with a modified SFTI inhibitor FCQR(N)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0022617biological_processextracellular matrix disassembly
A0030141cellular_componentsecretory granule
A0031214biological_processbiomineral tissue development
A0046872molecular_functionmetal ion binding
A0097186biological_processamelogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR CHAIN B OF TRYPSIN INHIBITOR 1
ChainResidue
ALEU40
AASP189
ASER190
ACYS191
AASN192
AGLY193
AASP194
ASER195
ASER214
APHE215
AGLY216
APHE41
ALYS217
AALA218
ACYS220
AHOH322
AHOH348
BHOH101
BHOH102
BHOH103
BHOH104
BHOH105
ACYS42
BHOH106
BHOH108
AHIS57
ATYR94
ALEU99
AMET151
ATYR172
ALEU175

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 Residues1
DetailsSITE: Reactive bond => ECO:0000250|UniProtKB:P81705
ChainResidueDetails
BARG5
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Cyclopeptide (Gly-Asp)
ChainResidueDetails
BGLY1
BASN14

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN159

226262

PDB entries from 2024-10-16

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