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3VHQ

Crystal structure of the Ca6 site mutant of Pro-SA-subtilisin

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 399
ChainResidue
AVAL108
AGLN110
AALA227
AGLU229
AHOH413
AHOH420

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AASP226
AHOH406
AHOH578
ALEU205
AASP208
AVAL210

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP212
AASP214
AASP216
AILE218
AASP222
AASP225

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP214
AASP216
AASP222
AASP224

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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