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3A3P

Crystal structure of complex between E201A/SA-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 1
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 2
ChainResidue
AALA227
AGLU229
AHOH48
AVAL108
AGLN110

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 3
ChainResidue
AASP119
AASP121
AASP314
AASP315
AHOH504
AHOH518

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 4
ChainResidue
AHOH45
AHOH51
ALEU205
AASP208
AVAL210
AASP226

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 5
ChainResidue
ACA6
AGLU91
AASP214
AASP216
AASP222

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 6
ChainResidue
ACA5
AASP212
AASP214
AASP216
AILE218
AASP222
AASP225

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 8
ChainResidue
AHOH41
AASP372
ALEU373
APRO375
AGLY377
AASP379

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 70
ChainResidue
BHIS28
BASP42
BHOH77
BHOH204

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

224572

PDB entries from 2024-09-04

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