Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8U3P

1.79 Angstrom resolution crystal structure of KatG from Mycobacterium tuberculosis with an MYW cofactor after heat incubation for 60 minutes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006979	biological_process	response to oxidative stress
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0016491	molecular_function	oxidoreductase activity
A	0016677	molecular_function	oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor
A	0020037	molecular_function	heme binding
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0045739	biological_process	positive regulation of DNA repair
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
A	0070301	biological_process	cellular response to hydrogen peroxide
A	0070402	molecular_function	NADPH binding
A	0070404	molecular_function	NADH binding
A	0098869	biological_process	cellular oxidant detoxification
B	0004096	molecular_function	catalase activity
B	0004601	molecular_function	peroxidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006979	biological_process	response to oxidative stress
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0016491	molecular_function	oxidoreductase activity
B	0016677	molecular_function	oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor
B	0020037	molecular_function	heme binding
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0045739	biological_process	positive regulation of DNA repair
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
B	0070301	biological_process	cellular response to hydrogen peroxide
B	0070402	molecular_function	NADPH binding
B	0070404	molecular_function	NADH binding
B	0098869	biological_process	cellular oxidant detoxification
C	0004096	molecular_function	catalase activity
C	0004601	molecular_function	peroxidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006979	biological_process	response to oxidative stress
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0016491	molecular_function	oxidoreductase activity
C	0016677	molecular_function	oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor
C	0020037	molecular_function	heme binding
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0045739	biological_process	positive regulation of DNA repair
C	0046677	biological_process	response to antibiotic
C	0046872	molecular_function	metal ion binding
C	0070301	biological_process	cellular response to hydrogen peroxide
C	0070402	molecular_function	NADPH binding
C	0070404	molecular_function	NADH binding
C	0098869	biological_process	cellular oxidant detoxification
D	0004096	molecular_function	catalase activity
D	0004601	molecular_function	peroxidase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006979	biological_process	response to oxidative stress
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0016491	molecular_function	oxidoreductase activity
D	0016677	molecular_function	oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor
D	0020037	molecular_function	heme binding
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0045739	biological_process	positive regulation of DNA repair
D	0046677	biological_process	response to antibiotic
D	0046872	molecular_function	metal ion binding
D	0070301	biological_process	cellular response to hydrogen peroxide
D	0070402	molecular_function	NADPH binding
D	0070404	molecular_function	NADH binding
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. TAALIVGGHTF

Chain	Residue	Details
A	THR262-PHE272

site_id	PS00436
Number of Residues	12
Details	PEROXIDASE_2 Peroxidases active site signature. GPlfIRMaWHAA

Chain	Residue	Details
A	GLY99-ALA110

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_01961

Chain	Residue	Details
A	HIS108
B	HIS108
C	HIS108
D	HIS108

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Tryptophan radical intermediate => ECO:0000269\|PubMed:18052167

Chain	Residue	Details
A	TRP321
B	TRP321
C	TRP321
D	TRP321

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: 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

Chain	Residue	Details
A	HIS270
B	HIS270
C	HIS270
D	HIS270

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000255\|HAMAP-Rule:MF_01961

Chain	Residue	Details
A	ARG104
B	ARG104
C	ARG104
D	ARG104

site_id	SWS_FT_FI5
Number of Residues	4
Details	CROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255); alternate => ECO:0000255\|HAMAP-Rule:MF_01961, ECO:0000269\|PubMed:15231843

Chain	Residue	Details
A	TRP107
B	TRP107
C	TRP107
D	TRP107

site_id	SWS_FT_FI6
Number of Residues	8
Details	CROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate => ECO:0000255\|HAMAP-Rule:MF_01961, ECO:0000269\|PubMed:15231843

Chain	Residue	Details
A	TYR229
A	MET255
B	TYR229
B	MET255
C	TYR229
C	MET255
D	TYR229
D	MET255

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)