Research workbench

Human erythrocyte catalase cryoem

Analyse Human erythrocyte catalase cryoem in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P8W
Type: protein
Length: 2,008 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catalase
EC: 1.11.1.6
UniProt: P04040
Ligands: NDP, HEM
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 35% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Catalase (EC 1.11.1.6)	protein	502	35% helix, 18% strand	P04040

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, D, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	673	0.88	0.92	52	empty
2	378	0.87	0.97	49	empty
3	385	0.87	0.96	50	empty
4	240	0.85	0.97	38	HEM
5	255	0.84	0.96	39	HEM

Interfaces

6 interfaces between chains.

B–C · 5022 Å² buried · 78 hydrogen bonds · protein-protein
A–D · 4992 Å² buried · 78 hydrogen bonds · protein-protein
A–B · 4727 Å² buried · 56 hydrogen bonds · protein-protein
C–D · 4726 Å² buried · 56 hydrogen bonds · protein-protein
A–C · 2087 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

7P8W · Human erythrocyte catalase cryoEM · the same entry in another collection · chain D against D, TM-score 1.00
P04040 · AlphaFold monomer V2.0 prediction for catalase (P04040) · a predicted model of the same protein · chain D against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P04040
Elsewhere: RCSB PDB 7P8W · PDBe 7P8W · UniProt P04040

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