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1TK2

Crystal Structure of the Complex formed between Alkaline Proteinase Savinase and Gramicidin S at 1.5A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1276
ChainResidue
AALA169
ATYR171
AALA174
AHOH2114
AHOH2137

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1277
ChainResidue
AILE79
AVAL81
AGLN2
AASP41
ALEU75
AASN77

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR CHAIN B OF GRAMICIDIN S
ChainResidue
ALEU96
AGLY100
AGLY102
AILE107
ALEU126
AGLY127
ASER128
APRO129
ASER130
AGLY154
AASN155
ASER166
AGLN191
ASER240
AHOH2127
BHOH2001

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues11
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIst.H
ChainResidueDetails
AVAL28-HIS39

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

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG
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
ChainResidueDetails
AASP32
AHIS64
ASER221

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AGLN2
AASP41
ALEU75
AASN77
AILE79
AVAL81
AALA169
ATYR171
AALA174

218853

PDB entries from 2024-04-24

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