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Cryo-EM structure of T275P katg from M. tuberculosis

Analyse Cryo-EM structure of T275P 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: 7A8Z
Type: protein
Length: 1,103 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catalase-peroxidase
EC: 1.11.1.21
UniProt: A0A0D5ZBI4
Pockets: 20 · best druggability 0.74

Structure

electron microscopy · 2 distinct chains · 45% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catalase-peroxidase (EC 1.11.1.21)	protein	553	44% helix, 4% strand	A0A0D5ZBI4
B	Catalase-peroxidase (EC 1.11.1.21)	protein	550	46% helix, 4% strand	A0A0D5ZBI4

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	962	0.74	0.77	83	empty
2	99	0.72	0.94	24	empty
3	773	0.71	0.77	68	empty
4	73	0.61	0.90	18	empty
5	115	0.60	0.86	30	empty

Interfaces

1 interface between chains.

A–B · 1706 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

7A8Z · Cryo-EM structure of T275P 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 7A8Z · PDBe 7A8Z · UniProt A0A0D5ZBI4

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