UniProt P04040

Catalase (P04040)

Catalase (UniProt P04040), EC 1.11.1.6: 24 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound, 426 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt: P04040
Protein: Catalase
EC: 1.11.1.6
Experimental structures: 24
Predicted models: 1
Ligands: 4
Pockets: 426 · 22 records with a druggable one

Structures

25 records of P04040 in the MolNFT archive: 24 experimental, 1 predicted.

Entry	Title	Method	Chains	Ligands	Pockets
1DGB	Human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM, NDP	20 (best 0.88)
1DGB	Human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM, NDP	20 (best 0.88)
1DGF	Human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM, NDP	20 (best 0.88)
1DGF	Human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM, NDP	20 (best 0.88)
1DGG	Human erythrocyte catalse cyanide complex	x-ray diffraction	A, B, C, D	CYN, HEM, NDP	20 (best 0.88)
1DGG	Human erythrocyte catalse cyanide complex	x-ray diffraction	A, B, C, D	CYN, HEM, NDP	20 (best 0.88)
1DGH	Human erythrocyte catalase 3-amino-1,2,4-triazole complex	x-ray diffraction	A, B, C, D	HEM, NDP	20 (best 0.88)
1DGH	Human erythrocyte catalase 3-amino-1,2,4-triazole complex	x-ray diffraction	A, B, C, D	HEM, NDP	20 (best 0.88)
1F4J	Structure of tetragonal crystals of human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM	20 (best 0.88)
1F4J	Structure of tetragonal crystals of human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM	20 (best 0.88)
1QQW	Crystal structure of human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM	20 (best 0.87)
1QQW	Crystal structure of human erythrocyte catalase	x-ray diffraction	A, B, C, D	HEM	20 (best 0.87)
7P8W	Human erythrocyte catalase cryoEM	electron microscopy	A, B, C, D	NDP, HEM	20 (best 0.88)
7P8W	Human erythrocyte catalase cryoem	electron microscopy	A, B, C, D	NDP, HEM	—
7VD9	2.29 A structure of the human catalase	electron microscopy	A, B, C, D	HEM, NDP	20 (best 0.87)
7VD9	2.29 a structure of the human catalase	electron microscopy	A, B, C, D	HEM, NDP	—
8EL9	Cryo-EM structure of human catalase	electron microscopy	A, B, C, D	HEM, NDP	20 (best 0.89)
8HID	HUMAN ERYTHROCYTE CATALSE COMPLEXED WITH BT-Br	x-ray diffraction	A, B, C, D	LLR, HEM	20 (best 0.88)
8PVD	Structure of catalase determined by cryoEM at 100 keV	electron microscopy	A	NDP, HEM	6 (best 0.75)
8SGV	human liver mitochondrial Catalase	electron microscopy	B, A, C, D	HEM, NDP	20 (best 0.87)
8WZH	Human erythrocyte catalase with SLS as additive during cryo-EM grid preparation	electron microscopy	B, A, C, D	HEM, NDP	20 (best 0.87)
8WZJ	Human erythrocyte catalase	electron microscopy	B, A, C, D	HEM, NDP	20 (best 0.88)
8WZK	Human erythrocyte catalase	electron microscopy	B, A, C, D	HEM, NDP	20 (best 0.88)
8WZM	Human erythrocyte catalase with CTAB as additive during EM sample preparation	electron microscopy	B, A, C, D	HEM, NDP	20 (best 0.88)
P04040	AlphaFold monomer V2.0 prediction for catalase (P04040)	predicted	A	—	—

Ligands

HEM · Protoporphyrin IX containing Fe · in 24 records
NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · in 19 records
CYN · Cyanide ion · in 2 records
LLR · (~{S})-azanyl-[2-[[3-bromanyl-4-(diethylamino)phenyl]methyl]hydrazinyl]methanethiol · in 1 record

Experiment against prediction

1DGF chain A against the predicted model P04040: TM-score 1.00, RMSD 0.24 Å
1DGF chain A against the predicted model P04040: TM-score 1.00, RMSD 0.24 Å
1DGG chain C against the predicted model P04040: TM-score 1.00, RMSD 0.27 Å
1DGG chain C against the predicted model P04040: TM-score 1.00, RMSD 0.27 Å
1DGF chain C against the predicted model P04040: TM-score 1.00, RMSD 0.27 Å
1DGF chain C against the predicted model P04040: TM-score 1.00, RMSD 0.27 Å
1DGF chain D against the predicted model P04040: TM-score 1.00, RMSD 0.27 Å
1DGF chain D against the predicted model P04040: TM-score 1.00, RMSD 0.27 Å
1DGG chain A against the predicted model P04040: TM-score 1.00, RMSD 0.28 Å
1DGG chain A against the predicted model P04040: TM-score 1.00, RMSD 0.28 Å

Elsewhere

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