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5SYJ

Crystal structure of the D141A variant of B. pseudomallei KatGin complex with isoniazid

Replaces:  4KWQ
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 Residues21
Detailsbinding site for residue HEM A 801
ChainResidue
AGLY104
ALYS283
ATHR284
AHIS285
ATHR323
ASER324
ATRP330
ATHR388
ATRP420
ANIZ810
AHOH924
ALEU105
AHOH976
AHOH990
ATRP111
AVAL239
ALEU274
AILE275
AGLY278
AHIS279
AGLY282

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 802
ChainResidue
AGLY122
AARG123
AGLY124
ASER494
AHOH1148
AHOH1368

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 803
ChainResidue
AGLY124
AGLU198
AVAL200
ANIZ809
AHOH1368

site_idAC4
Number of Residues3
Detailsbinding site for residue MPD A 804
ChainResidue
APRO154
ALYS158
AHOH1266

site_idAC5
Number of Residues3
Detailsbinding site for residue MPD A 805
ChainResidue
ALEU209
AVAL293
ATHR323

site_idAC6
Number of Residues5
Detailsbinding site for residue MPD A 806
ChainResidue
ATYR719
AASP731
AHOH1012
BMET62
BHOH916

site_idAC7
Number of Residues3
Detailsbinding site for residue PO4 A 807
ChainResidue
ALYS380
AHIS381
AARG382

site_idAC8
Number of Residues2
Detailsbinding site for residue MPD A 808
ChainResidue
AASP663
AASN667

site_idAC9
Number of Residues11
Detailsbinding site for residue NIZ A 809
ChainResidue
AARG123
AGLU128
AGLU198
AASP199
AVAL200
AGLY493
ASER494
AGLN622
ATHR625
ACL803
AHOH949

site_idAD1
Number of Residues7
Detailsbinding site for residue NIZ A 810
ChainResidue
AARG108
ATRP111
AHIS112
AALA141
AHEM801
AHOH956
AHOH1059

site_idAD2
Number of Residues21
Detailsbinding site for residue HEM B 801
ChainResidue
BGLY104
BLEU105
BTRP111
BVAL239
BLEU274
BILE275
BGLY278
BHIS279
BGLY282
BLYS283
BTHR284
BHIS285
BTHR323
BSER324
BTRP330
BTHR388
BTRP420
BNIZ810
BHOH940
BHOH963
BHOH1074

site_idAD3
Number of Residues6
Detailsbinding site for residue NA B 802
ChainResidue
BGLY122
BARG123
BGLY124
BSER494
BHOH971
BHOH1345

site_idAD4
Number of Residues5
Detailsbinding site for residue CL B 803
ChainResidue
BGLY124
BGLU198
BVAL200
BNIZ809
BHOH1345

site_idAD5
Number of Residues2
Detailsbinding site for residue MPD B 804
ChainResidue
BSER324
BTHR323

site_idAD6
Number of Residues6
Detailsbinding site for residue MPD B 805
ChainResidue
BTRP362
BGLY567
BHIS568
BALA569
BGLU726
BHOH1305

site_idAD7
Number of Residues3
Detailsbinding site for residue MPD B 806
ChainResidue
BASN741
BLEU742
BARG744

site_idAD8
Number of Residues5
Detailsbinding site for residue MPD B 807
ChainResidue
BGLU351
BLEU352
BLYS365
BLYS564
BGLY567

site_idAD9
Number of Residues2
Detailsbinding site for residue PO4 B 808
ChainResidue
BHIS381
BARG382

site_idAE1
Number of Residues8
Detailsbinding site for residue NIZ B 809
ChainResidue
BARG123
BGLU128
BGLU198
BVAL200
BGLY493
BGLN622
BCL803
BHOH992

site_idAE2
Number of Residues9
Detailsbinding site for residue NIZ B 810
ChainResidue
BARG108
BTRP111
BHIS112
BALA141
BPRO241
BSER324
BHEM801
BHOH914
BHOH1072

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

224572

PDB entries from 2024-09-04

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