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3A3O

Crystal structure of complex between SA-subtilisin and Tk-propeptide with deletion of the five C-terminal residues

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 1
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 2
ChainResidue
AASP208
AVAL210
AASP226
AHOH37
AHOH57
ALEU205

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 3
ChainResidue
ACA4
AASP212
AASP214
AASP216
AILE218
AASP222
AASP225

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 4
ChainResidue
ACA3
AGLU91
AASP214
AASP216
AASP222

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 5
ChainResidue
AHOH26
AVAL108
AGLN110
AALA227
AGLU229
AHOH579

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 6
ChainResidue
AHOH55
AASP372
ALEU373
APRO375
AGLY377
AASP379

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 7
ChainResidue
AASP119
AASP121
AASP314
AASP315
AHOH471
AHOH479

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 65
ChainResidue
BHIS28
BASP42
BHOH67
BHOH105

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

221371

PDB entries from 2024-06-19

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