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1A2Q

SUBTILISIN BPN' MUTANT 7186

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_id169
Number of Residues1
DetailsMUTATION FROM GLY TO ALA AT RESIDUE 169.
ChainResidue
AALA169

site_id218
Number of Residues1
DetailsMUTATION FROM ASN TO SER AT RESIDUE 218.
ChainResidue
ASER218

site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 295
ChainResidue
AASN77
AILE79
AVAL81
AGLN2
AASP41
ALEU75

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 296
ChainResidue
AALA169
ATYR171
AVAL174
AHOH340
AHOH372

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACN A 290
ChainResidue
AVAL44
APHE58
AARG186

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACN A 291
ChainResidue
ASER145
APHE189
ASER218

site_idC22
Number of Residues1
DetailsMUTATION FROM THR TO CYS AT RESIDUE 22. CYS 22 FORMS A DISULFIDE BOND WITH CYS 87.
ChainResidue
ACYS22

site_idC87
Number of Residues1
DetailsMUTATION FROM SER TO CYS AT RESIDUE 87. CYS 87 FORMS A DISULFIDE BOND WITH CYS 22.
ChainResidue
ACYS87

site_idCA1
Number of Residues1
DetailsHIGH AFFINITY CALCIUM BINDING SITE.
ChainResidue
ACA295

site_idCA2
Number of Residues1
DetailsLOW AFFINITY CALCIUM BINDING SITE.
ChainResidue
ACA296

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH
ChainResidueDetails
AVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA
ChainResidueDetails
AHIS64-ALA74

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG
ChainResidueDetails
AGLY219-GLY229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818
ChainResidueDetails
AASP32
AHIS64
AMIS221

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AGLN2
AASP41
ALEU75
AASN77
AILE79
AVAL81
AALA169
ATYR171
AVAL174

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
AHIS64
AASP32

site_idMCSA1
Number of Residues4
DetailsM-CSA 723
ChainResidueDetails
AASP32electrostatic interaction, electrostatic stabiliser
AHIS64proton acceptor, proton donor
AASN155electrostatic interaction, electrostatic stabiliser
AMIS221nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-07-10

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