Research workbench

Mycobacterium tuberculosis HigA2 (Form III)

Analyse Mycobacterium tuberculosis HigA2 (Form III) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EWE
Type: protein
Length: 352 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.41
Source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Molecule: Putative antitoxin HigA2
UniProt: O53467
Pockets: 4 · best druggability 0.48

Structure

x-ray diffraction · resolution 3.41 · 4 distinct chains · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative antitoxin HigA2	protein	71	46% helix, 14% strand	O53467
B, C	Putative antitoxin HigA2	protein	70	36% helix, 20% strand	O53467
D	Putative antitoxin HigA2	protein	69	42% helix, 12% strand	O53467
E	Putative antitoxin HigA2	protein	72	43% helix, 11% strand	O53467

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.48	0.85	17	empty
2	50	0.44	0.84	17	empty
3	60	0.26	0.73	13	empty
4	51	0.24	0.73	14	empty

Interfaces

8 interfaces between chains.

A–B · 1323 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 1321 Å² buried · 25 hydrogen bonds · protein-protein
B–E · 409 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 290 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 116 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7EWE · Mycobacterium tuberculosis HIGA2 (form III) · the same entry in another collection · chain E against E, TM-score 1.00
O53467 · AlphaFold monomer V2.0 prediction for putative antitoxin HIGA2 (O53467) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 O53467
Elsewhere: RCSB PDB 7EWE · PDBe 7EWE · UniProt O53467

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