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3WQB

Crystal structure of aeromonas sobria serine protease (ASP) and the chaperone (ORF2) complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 901
ChainResidue
AASN29
AASP87
AVAL126
AASN128
AILE130
ATHR132

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 902
ChainResidue
AALA555
AASN578
AASN579
AASP454
AASP488
AASP553

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 903
ChainResidue
AASP297
ALEU298
AGLY300
AMET303
AASN306
ACYS326

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVVDDGLaiaH
ChainResidueDetails
AVAL74-HIS85

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTsVSGiIAA
ChainResidueDetails
AHIS115-ALA125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP78
AHIS115
AALA336

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:19654332, ECO:0000269|PubMed:25784551, ECO:0007744|PDB:3HJR, ECO:0007744|PDB:3WQB
ChainResidueDetails
AASN29
AMET303
AASN306
ACYS326
AASP454
AASP488
AASP553
AALA555
AASN578
AASN579
AASP87
AVAL126
AASN128
AILE130
ATHR132
AASP297
ALEU298
AGLY300

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PDB entries from 2024-07-24

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