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5SX0

Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH7.5

Replaces:  2B2S
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
ATHR284
AHIS285
ATHR323
ASER324
ATRP330
ATHR388
AOXY803
AOXY804
AO805
AHOH1006
ALEU105
AHOH1119
AHOH1128
ATRP111
ALEU274
AILE275
AGLY278
AHIS279
AGLY282
ALYS283

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 802
ChainResidue
AGLY122
AARG123
AGLY124
ASER494
AHOH915
AHOH1257

site_idAC3
Number of Residues6
Detailsbinding site for residue OXY A 803
ChainResidue
AARG108
AHIS112
AHEM801
AOXY804
AO805
AHOH901

site_idAC4
Number of Residues7
Detailsbinding site for residue OXY A 804
ChainResidue
ATRP111
AHIS112
AHEM801
AOXY803
AO805
AHOH964
AHOH1342

site_idAC5
Number of Residues5
Detailsbinding site for residue O A 805
ChainResidue
ATRP111
AHIS112
AHEM801
AOXY803
AOXY804

site_idAC6
Number of Residues2
Detailsbinding site for residue MPD A 806
ChainResidue
ATHR323
ASER324

site_idAC7
Number of Residues2
Detailsbinding site for residue MPD A 807
ChainResidue
APRO154
AHOH1065

site_idAC8
Number of Residues10
Detailsbinding site for residue TRS A 808
ChainResidue
AALA120
AASP121
AARG492
AVAL593
ALEU594
ALYS620
ALEU623
AHOH933
AHOH1073
AHOH1077

site_idAC9
Number of Residues22
Detailsbinding site for residue HEM B 801
ChainResidue
BGLY104
BLEU105
BTRP111
BPRO241
BLEU274
BILE275
BGLY278
BHIS279
BGLY282
BLYS283
BTHR284
BHIS285
BTHR323
BSER324
BTRP330
BTHR388
BTRP420
BOXY803
BO804
BHOH1986
BHOH2051
BHOH2102

site_idAD1
Number of Residues6
Detailsbinding site for residue NA B 802
ChainResidue
BGLY122
BARG123
BGLY124
BSER494
BHOH2025
BHOH2233

site_idAD2
Number of Residues5
Detailsbinding site for residue OXY B 803
ChainResidue
BARG108
BHIS112
BHEM801
BO804
BHOH1905

site_idAD3
Number of Residues5
Detailsbinding site for residue O B 804
ChainResidue
BTRP111
BHIS112
BHEM801
BOXY803
BHOH1941

site_idAD4
Number of Residues2
Detailsbinding site for residue MPD B 805
ChainResidue
BTHR323
BSER324

site_idAD5
Number of Residues11
Detailsbinding site for residue TRS B 806
ChainResidue
BALA120
BASP121
BARG492
BVAL593
BLYS620
BLEU623
BHOH1915
BHOH1916
BHOH1963
BHOH2077
BHOH2105

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TVALIAGGHTF
ChainResidueDetails
ATHR271-PHE281
BTHR271-PHE281

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GGlfIRMaWHSA
ChainResidueDetails
AGLY103-ALA114
BGLY103-ALA114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
BHIS112

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
BHIS279

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
BARG108

site_idSWS_FT_FI4
Number of Residues1
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
BTRP111

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
BTYR238
BMET264

222036

PDB entries from 2024-07-03

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