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2Z2Z

Crystal structure of unautoprocessed form of Tk-subtilisin soaked by 10mM CaCl2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AVAL108
AGLN110
AALA227
AGLU229
AHOH1405
AHOH1408

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AASP315
AHOH1086
AHOH1350
AASP119
AASP121
AASP314

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
ALEU205
AASP208
AVAL210
AASP226
AHOH1008
AHOH1010

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
AASP214
AASP216
AASP222
AASP224
AHOH1385
AHOH1406

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1006
ChainResidue
AASP372
ALEU373
APRO375
AGLY377
AASP379
AHOH1066

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1007
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

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 Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP115
AHIS153
AALA324

223166

PDB entries from 2024-07-31

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