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5AQE

Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1277
ChainResidue
AVAL104
ASER132
AALA133
ATHR134
AHOH2020
AHOH2441
AHOH2442

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1278
ChainResidue
ALEU75
AASN77
AILE79
AVAL81
AGLN2
AASP41

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1279
ChainResidue
AGLY163
AASN252
ATHR253
AALA254
AHOH2353
AHOH2407
AHOH2414
AHOH2419
AHOH2437
AHOH2439

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1280
ChainResidue
ATRP241
AGLN245
AHIS249
AASN252
AHOH2390
AHOH2392
AHOH2400
AHOH2402
AHOH2443

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 1281
ChainResidue
AGLN12
APRO14
AALA15
AHOH2036
AHOH2046
AHOH2053

site_idAC6
Number of Residues11
DetailsBinding site for Ligand VOD A1276 bound to SER A 221
ChainResidue
AHIS64
ALEU126
AGLY127
AALA152
AGLY154
AASN155
AGLY219
ATHR220
ASER221
AHOH2178
AHOH2253

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 Residues263
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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