Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5KQ2

Crystal structure of the A357D 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 Residues22
Detailsbinding site for residue HEM A 801
ChainResidue
AGLY104
AHIS279
AGLY282
ALYS283
ATHR284
AHIS285
ATHR323
ASER324
ATRP330
ATHR388
AOXY804
ALEU105
AHOH926
AHOH973
AHOH1112
AILE107
ATOX111
AVAL239
APRO241
ALEU274
AILE275
AGLY278

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 802
ChainResidue
AGLY122
AARG123
AGLY124
ASER494
AHOH1174
AHOH1432

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 803
ChainResidue
AGLY124
AGLU198
AVAL200
AHOH1432
AHOH1566

site_idAC4
Number of Residues7
Detailsbinding site for residue OXY A 804
ChainResidue
AARG108
ATOX111
AHIS112
AASP141
AHEM801
AHOH1017
AHOH1068

site_idAC5
Number of Residues3
Detailsbinding site for residue PO4 A 805
ChainResidue
AHIS381
AARG382
AHOH995

site_idAC6
Number of Residues5
Detailsbinding site for residue MPD A 806
ChainResidue
ATRP362
APHE394
AHOH1255
BHOH1309
BHOH1522

site_idAC7
Number of Residues4
Detailsbinding site for residue MPD A 807
ChainResidue
ALEU209
ATHR323
ASER324
AHOH1515

site_idAC8
Number of Residues4
Detailsbinding site for residue MPD A 808
ChainResidue
AASP83
APRO154
AHOH1331
AHOH1423

site_idAC9
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
BHOH1011
BHOH1013
BHOH1119

site_idAD1
Number of Residues6
Detailsbinding site for residue NA B 802
ChainResidue
BGLY122
BARG123
BGLY124
BSER494
BHOH1063
BHOH1442

site_idAD2
Number of Residues5
Detailsbinding site for residue CL B 803
ChainResidue
BGLY124
BGLU198
BVAL200
BHOH1442
BHOH1564

site_idAD3
Number of Residues6
Detailsbinding site for residue OXY B 804
ChainResidue
BARG108
BTOX111
BHIS112
BASP141
BHEM801
BHOH906

site_idAD4
Number of Residues4
Detailsbinding site for residue PO4 B 805
ChainResidue
BLYS380
BHIS381
BARG382
BHOH1089

site_idAD5
Number of Residues3
Detailsbinding site for residue MPD B 806
ChainResidue
BASP357
BTHR323
BSER324

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon