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4C50

Crystal Structure of the Catalase-Peroxidase (KatG) D137S mutant from Mycobacterium Tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006979biological_processresponse to oxidative stress
A0009274cellular_componentpeptidoglycan-based cell wall
A0016677molecular_functionoxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0045739biological_processpositive regulation of DNA repair
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0070301biological_processcellular response to hydrogen peroxide
A0070402molecular_functionNADPH binding
A0070404molecular_functionNADH binding
A0098869biological_processcellular oxidant detoxification
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006979biological_processresponse to oxidative stress
B0009274cellular_componentpeptidoglycan-based cell wall
B0016677molecular_functionoxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor
B0020037molecular_functionheme binding
B0042744biological_processhydrogen peroxide catabolic process
B0045739biological_processpositive regulation of DNA repair
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0070301biological_processcellular response to hydrogen peroxide
B0070402molecular_functionNADPH binding
B0070404molecular_functionNADH binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TAALIVGGHTF
ChainResidueDetails
ATHR262-PHE272

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GPlfIRMaWHAA
ChainResidueDetails
AGLY99-ALA110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
AHIS108
BHIS108

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:18052167
ChainResidueDetails
ATRP321
BTRP321

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:15231843, ECO:0000269|PubMed:16566587, ECO:0000269|PubMed:24185282, ECO:0007744|PDB:1SJ2, ECO:0007744|PDB:2CCA, ECO:0007744|PDB:2CCD, ECO:0007744|PDB:4C51
ChainResidueDetails
AHIS270
BHIS270

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
ChainResidueDetails
AARG104
BARG104

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
ChainResidueDetails
ATRP107
BTRP107

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
ChainResidueDetails
ATYR229
AMET255
BTYR229
BMET255

227111

PDB entries from 2024-11-06

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