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Cryo-EM structure of W107R katg from M. tuberculosis

Analyse Cryo-EM structure of W107R katg from M. tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A2I
Type: protein
Length: 1,217 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catalase-peroxidase
EC: 1.11.1.21
UniProt: A0A0D5ZBI4
Ligands: HEM
Pockets: 19 · best druggability 0.82

Structure

electron microscopy · 2 distinct chains · 42% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catalase-peroxidase (EC 1.11.1.21)	protein	563	43% helix, 3% strand	A0A0D5ZBI4
B	Catalase-peroxidase (EC 1.11.1.21)	protein	654	42% helix, 6% strand	A0A0D5ZBI4

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains B

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

Pockets

19 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	805	0.82	0.84	76	HEM
2	248	0.73	0.87	33	empty
3	606	0.71	0.79	73	empty
4	669	0.67	0.76	72	empty
5	394	0.65	0.79	52	empty

Interfaces

1 interface between chains.

A–B · 2480 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

7A2I · Cryo-EM structure of W107R KatG from M. tuberculosis · the same entry in another collection · chain A 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 A0A0D5ZBI4
Elsewhere: RCSB PDB 7A2I · PDBe 7A2I · UniProt A0A0D5ZBI4

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