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2Z30

Crystal structure of complex form between mat-Tk-subtilisin and Tk-propeptide

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
ALEU205
AASP208
AVAL210
AASP226
AHOH1009
AHOH1202

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AILE218
AASP222
AASP225
ACA1003
AHOH1379
AASP212
AASP214
AASP216

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AGLU91
AASP214
AASP216
AASP222
ACA1002

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AVAL108
AGLN110
AALA227
AGLU229
AHOH1035
AHOH1321

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1005
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1006
ChainResidue
AASP372
ALEU373
APRO375
AGLY377
AASP379
AHOH1019

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1007
ChainResidue
AASP119
AASP121
AASP314
AASP315

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 2001
ChainResidue
BHIS28
BASP42
BHOH2064

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

219869

PDB entries from 2024-05-15

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