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5KQI

Crystal structure of the L326D variant of catalase-peroxidase from B. pseudomallei

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 Residues19
Detailsbinding site for residue HEM A 801
ChainResidue
AGLY104
ATHR284
AHIS285
ATHR323
ASER324
ATRP330
ATHR388
AOXY804
AHOH954
AHOH975
AHOH1030
ALEU105
ATOX111
AVAL239
ALEU274
AGLY278
AHIS279
AGLY282
ALYS283

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 802
ChainResidue
AGLY122
AARG123
AGLY124
ASER494
AHOH1012
AHOH1379

site_idAC3
Number of Residues6
Detailsbinding site for residue CL A 803
ChainResidue
AGLY124
AGLU198
AVAL200
AHOH1379
AHOH1430
AHOH1482

site_idAC4
Number of Residues7
Detailsbinding site for residue OXY A 804
ChainResidue
AARG108
ATOX111
AHIS112
AASP141
AHEM801
AHOH950
AHOH1257

site_idAC5
Number of Residues5
Detailsbinding site for residue PO4 A 805
ChainResidue
ALYS379
ALYS380
AHIS381
AARG382
AHOH1181

site_idAC6
Number of Residues3
Detailsbinding site for residue MPD A 807
ChainResidue
AASP83
APRO154
AHOH1373

site_idAC7
Number of Residues2
Detailsbinding site for residue MPD A 808
ChainResidue
AASP663
AVAL666

site_idAC8
Number of Residues20
Detailsbinding site for residue HEM B 801
ChainResidue
BGLY104
BLEU105
BILE107
BTOX111
BVAL239
BLEU274
BGLY278
BHIS279
BGLY282
BLYS283
BTHR284
BHIS285
BTHR323
BSER324
BTRP330
BTHR388
BOXY804
BHOH916
BHOH1050
BHOH1142

site_idAC9
Number of Residues6
Detailsbinding site for residue NA B 802
ChainResidue
BGLY122
BARG123
BGLY124
BSER494
BHOH929
BHOH1217

site_idAD1
Number of Residues6
Detailsbinding site for residue OXY B 804
ChainResidue
BARG108
BTOX111
BHIS112
BASP141
BHEM801
BHOH906

site_idAD2
Number of Residues4
Detailsbinding site for residue PO4 B 805
ChainResidue
BLYS380
BHIS381
BARG382
BHOH997

site_idAD3
Number of Residues4
Detailsbinding site for residue MPD B 806
ChainResidue
BALA290
BTHR323
BSER324
BHOH1212

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

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
ATOX111
BTOX111

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

219140

PDB entries from 2024-05-01

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