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

6SKB

Crystal Structure of Human Kallikrein 6 (N217D/I218Y/K224R) in complex with GSK3496783A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue LH5 A 301
ChainResidue
ALEU41
AVAL213
ATRP215
AGLY216
AASP217
ATYR218
ACYS220
AGLY226
ARH5302
AHOH459
AHOH471
AHIS57
AASP189
ASER190
ACYS191
AGLN192
AGLY193
AASP194
ASER195

site_idAC2
Number of Residues15
Detailsbinding site for residue RH5 A 302
ChainResidue
ALEU41
AHIS57
AASP189
ASER190
ACYS191
AGLN192
AGLY193
AASP194
ASER195
AGLY216
AASP217
ATYR218
ACYS220
ALH5301
AHOH471

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL C 303
ChainResidue
APRO92
AASP93
CTYR34
CPHE66
CLYS70
CLEU73
CHOH449

site_idAC4
Number of Residues20
Detailsbinding site for residue LH5 C 302
ChainResidue
AGLY38
CLEU41
CHIS57
CASP189
CSER190
CCYS191
CGLN192
CGLY193
CASP194
CSER195
CVAL213
CTRP215
CGLY216
CASP217
CTYR218
CCYS220
CRH5301
CHOH459
CHOH487
CHOH505

site_idAC5
Number of Residues19
Detailsbinding site for Di-peptide LH5 B 301 and SER B 195
ChainResidue
BLEU41
BCYS42
BGLY43
BHIS57
BASP189
BSER190
BCYS191
BGLY193
BASP194
BGLY196
BGLY197
BVAL213
BTRP215
BGLY216
BASP217
BTYR218
BCYS220
BRH5302
BHOH422

site_idAC6
Number of Residues18
Detailsbinding site for Di-peptide RH5 B 302 and SER B 195
ChainResidue
BLEU41
BCYS42
BGLY43
BHIS57
BASP189
BSER190
BCYS191
BGLY193
BASP194
BGLY196
BGLY197
BVAL213
BTRP215
BGLY216
BASP217
BTYR218
BCYS220
BLH5301

site_idAC7
Number of Residues21
Detailsbinding site for Di-peptide RH5 C 301 and SER C 195
ChainResidue
CLEU41
CCYS42
CGLY43
CHIS57
CCYS58
CASP189
CSER190
CCYS191
CGLN192
CGLY193
CASP194
CGLY196
CGLY197
CVAL213
CGLY216
CASP217
CTYR218
CCYS220
CLH5302
CHOH505
AGLY38

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. DScqGDSGGPLV
ChainResidueDetails
AASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:12016211
ChainResidueDetails
AHIS57
AASP102
ASER195
BHIS57
BASP102
BSER195
CHIS57
CASP102
CSER195

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Cleavage; by autolysis
ChainResidueDetails
AGLN76
BGLN76
CGLN76

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLN132
BGLN132
CGLN132

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon