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2Z2Y

Crystal structure of autoprocessed form of Tk-subtilisin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AASP226
AHOH2081
AHOH2130
ALEU205
AASP208
AVAL210

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP212
AASP214
AASP216
AILE218
AASP222
AASP225
ACA1004

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AASP214
AASP216
AASP222
ACA1003
DHIS20

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1005
ChainResidue
AVAL108
AGLN110
AALA227
AGLU229
AHOH2008
AHOH2195

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1006
ChainResidue
AASP372
ALEU373
APRO375
AGLY377
AASP379
AHOH2036

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1007
ChainResidue
AASP119
AASP121
AASP314
AASP315
AHOH2152
AHOH2221

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1008
ChainResidue
CGLN84
CASP124
CLEU164
CASN166
CILE168
CVAL170

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1009
ChainResidue
CLEU205
CASP208
CVAL210
CASP226
CHOH2063
CHOH2085

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA C 1010
ChainResidue
CASP212
CASP214
CASP216
CILE218
CASP222
CASP225
CCA1011

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 1011
ChainResidue
BHIS20
CASP214
CASP216
CASP222
CCA1010

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1012
ChainResidue
CVAL108
CGLN110
CALA227
CGLU229
CHOH2013
CHOH2180

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1013
ChainResidue
CASP372
CLEU373
CPRO375
CGLY377
CASP379
CHOH2028

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1014
ChainResidue
CASP119
CASP121
CASP314
CASP315
CHOH2095
CHOH2193

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2001
ChainResidue
AHIS153
ACYS324
BLEU69
BHOH2027

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2002
ChainResidue
BGLU61
BHIS64
BHOH2037
CGLU318

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 2003
ChainResidue
CHIS153
CCYS324
DLEU69
DHOH2034

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 2004
ChainResidue
DHIS64
AGLU318
AHOH2005
DGLU61

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 2005
ChainResidue
CHOH2184
DHIS28
DASP42

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 2006
ChainResidue
AHOH2257
BHIS28
BASP42

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGVdydH
ChainResidueDetails
AVAL111-HIS122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP115
AHIS153
ACYS324
CASP115
CHIS153
CCYS324

223166

PDB entries from 2024-07-31

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