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5KSN

Crystal structure of the S324G variant of catalase-peroxidase from B. pseudomallei with INH bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0070301biological_processcellular response to hydrogen peroxide
A0098869biological_processcellular oxidant detoxification
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0070301biological_processcellular response to hydrogen peroxide
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue HEM A 801
ChainResidue
AGLY104
ALYS283
ATHR284
AHIS285
ATHR323
AGLY324
ATRP330
ATHR388
ATRP420
AOXY804
AOXY805
ALEU105
AHOH911
AHOH962
AHOH1008
AHOH1025
AHOH1123
AHOH1543
ATRP111
AVAL239
ALEU274
AILE275
AGLY278
AHIS279
AGLY282

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 802
ChainResidue
AGLY122
AARG123
AGLY124
ASER494
AHOH1080
AHOH1468

site_idAC3
Number of Residues6
Detailsbinding site for residue CL A 803
ChainResidue
AGLY124
AGLU198
AVAL200
ANIZ809
AHOH1468
AHOH1623

site_idAC4
Number of Residues7
Detailsbinding site for residue OXY A 804
ChainResidue
AARG108
AHIS112
AASP141
AHEM801
AOXY805
AHOH911
AHOH972

site_idAC5
Number of Residues6
Detailsbinding site for residue OXY A 805
ChainResidue
ATRP111
AHIS112
AHEM801
AOXY804
AHOH911
AHOH1121

site_idAC6
Number of Residues3
Detailsbinding site for residue PO4 A 806
ChainResidue
AHIS381
AARG382
AHOH1230

site_idAC7
Number of Residues2
Detailsbinding site for residue MPD A 807
ChainResidue
ATHR323
AHOH1644

site_idAC8
Number of Residues5
Detailsbinding site for residue MPD A 808
ChainResidue
AASP83
APRO154
AHOH1367
AHOH1518
AHOH1645

site_idAC9
Number of Residues11
Detailsbinding site for residue NIZ A 809
ChainResidue
AARG123
AGLU128
AGLU198
AASP199
AGLY493
ASER494
AGLN622
ALEU623
ATHR625
ACL803
AHOH1206

site_idAD1
Number of Residues23
Detailsbinding site for residue HEM B 801
ChainResidue
BGLY104
BLEU105
BTRP111
BVAL239
BLEU274
BILE275
BGLY278
BHIS279
BGLY282
BLYS283
BTHR284
BHIS285
BTHR323
BGLY324
BTRP330
BTHR388
BOXY804
BOXY805
BHOH908
BHOH964
BHOH1007
BHOH1017
BHOH1200

site_idAD2
Number of Residues6
Detailsbinding site for residue NA B 802
ChainResidue
BHOH1468
BGLY122
BARG123
BGLY124
BSER494
BHOH1050

site_idAD3
Number of Residues4
Detailsbinding site for residue CL B 803
ChainResidue
BGLY124
BGLU198
BVAL200
BNIZ809

site_idAD4
Number of Residues8
Detailsbinding site for residue OXY B 804
ChainResidue
BARG108
BHIS112
BASP141
BHEM801
BOXY805
BHOH908
BHOH911
BHOH914

site_idAD5
Number of Residues7
Detailsbinding site for residue OXY B 805
ChainResidue
BTRP111
BHIS112
BHEM801
BOXY804
BHOH908
BHOH911
BHOH1343

site_idAD6
Number of Residues5
Detailsbinding site for residue PO4 B 806
ChainResidue
BHIS381
BARG382
BHOH1088
BHOH1204
BHOH1453

site_idAD7
Number of Residues3
Detailsbinding site for residue MPD B 807
ChainResidue
BTHR323
BGLY324
BHOH1155

site_idAD8
Number of Residues6
Detailsbinding site for residue MPD B 808
ChainResidue
BTRP362
BGLY567
BHIS568
BALA569
BGLU726
BHOH1086

site_idAD9
Number of Residues10
Detailsbinding site for residue NIZ B 809
ChainResidue
BARG123
BGLU128
BGLU198
BASP199
BGLY493
BSER494
BGLN622
BTHR625
BCL803
BHOH1043

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TVALIAGGHTF
ChainResidueDetails
ATHR271-PHE281

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GGlfIRMaWHSA
ChainResidueDetails
AGLY103-ALA114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
AHIS112
BHIS112

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
AHIS279
BHIS279

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
AARG108
BARG108

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
ATRP111
BTRP111

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
ATYR238
AMET264
BTYR238
BMET264

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PDB entries from 2024-08-07

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