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

2Z2X

Crystal structure of mature form of Tk-subtilisin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AASP372
ALEU373
APRO375
AGLY377
AASP379
AHOH1269

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AASN166
AILE168
AVAL170
AGLN84
AASP124
ALEU164

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP214
AASP216
AASP222
AASP224
AHOH1272
AHOH1273

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AASP212
AASP214
AASP216
AILE218
AASP222
AASP225

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1005
ChainResidue
ALEU205
AASP208
AVAL210
AASP226
AHOH1268
AHOH1271

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1006
ChainResidue
AVAL108
AGLN110
AALA227
AGLU229
AHOH1266
AHOH1267

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1007
ChainResidue
AASP119
AASP121
AASP314
AASP315
AHOH1017
AHOH1270

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

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVSG
ChainResidueDetails
AGLY322-GLY332

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP115
AHIS153
AMIS324

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
AASP115
AHIS153

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon