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

6CFQ

Crystal structure of the D141N 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 Residues21
Detailsbinding site for residue HEM A 801
ChainResidue
AGLY104
ALYS283
ATHR284
AHIS285
ATHR323
ASER324
ATHR388
AOXY804
AOXY808
AHOH906
AHOH961
ALEU105
AHOH1024
AHOH1083
ATRP111
AVAL239
ALEU274
AILE275
AGLY278
AHIS279
AGLY282

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 802
ChainResidue
AGLY122
AARG123
AGLY124
ASER494
AHOH1011
AHOH1495

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 803
ChainResidue
AGLY124
AGLU198
AVAL200
AHOH1495
AHOH1650

site_idAC4
Number of Residues7
Detailsbinding site for residue OXY A 804
ChainResidue
AARG108
AHIS112
AASN141
AHEM801
AOXY808
AHOH906
AHOH977

site_idAC5
Number of Residues4
Detailsbinding site for residue PO4 A 805
ChainResidue
ALYS380
AHIS381
AARG382
AHOH1345

site_idAC6
Number of Residues1
Detailsbinding site for residue MPD A 806
ChainResidue
ATHR323

site_idAC7
Number of Residues4
Detailsbinding site for residue MPD A 807
ChainResidue
AASP83
APRO154
AHOH1181
AHOH1506

site_idAC8
Number of Residues6
Detailsbinding site for residue OXY A 808
ChainResidue
ATRP111
AHIS112
AHEM801
AOXY804
AHOH906
AHOH1223

site_idAC9
Number of Residues23
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
BOXY804
BOXY807
BHOH910
BHOH991
BHOH1010
BHOH1091

site_idAD1
Number of Residues6
Detailsbinding site for residue NA B 802
ChainResidue
BGLY122
BARG123
BGLY124
BSER494
BHOH1088
BHOH1486

site_idAD2
Number of Residues6
Detailsbinding site for residue CL B 803
ChainResidue
BGLY124
BGLU198
BVAL200
BNIZ809
BHOH1486
BHOH1628

site_idAD3
Number of Residues7
Detailsbinding site for residue OXY B 804
ChainResidue
BARG108
BHIS112
BASN141
BHEM801
BOXY807
BHOH910
BHOH942

site_idAD4
Number of Residues4
Detailsbinding site for residue PO4 B 805
ChainResidue
BHOH1014
BLYS380
BHIS381
BARG382

site_idAD5
Number of Residues3
Detailsbinding site for residue MPD B 806
ChainResidue
BALA290
BTHR323
BSER324

site_idAD6
Number of Residues6
Detailsbinding site for residue OXY B 807
ChainResidue
BTRP111
BHIS112
BHEM801
BOXY804
BHOH910
BHOH1210

site_idAD7
Number of Residues5
Detailsbinding site for residue MPD B 808
ChainResidue
BTRP362
BPHE394
BHIS568
BALA569
BGLU726

site_idAD8
Number of Residues11
Detailsbinding site for residue NIZ B 809
ChainResidue
BARG123
BGLU128
BGLU198
BASP199
BGLY493
BSER494
BGLN622
BLEU623
BTHR625
BCL803
BHOH993

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
ChainResidueDetails
AHIS112
BHIS112

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS279
BHIS279

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG108
BARG108

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)
ChainResidueDetails
ATRP111
BTRP111

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91)
ChainResidueDetails
ATYR238
AMET264
BTYR238
BMET264

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon