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Crystal structure of RV0371C from mycobacterium tuberculosis H37RV

Analyse Crystal structure of RV0371C from mycobacterium tuberculosis H37RV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WEE
Type: protein
Length: 383 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Moba-related protein
UniProt: O53706
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Moba-related protein	protein	189	34% helix, 26% strand	O53706
B	Moba-related protein	protein	194	32% helix, 26% strand	O53706

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	280	0.62	0.80	38	GOL
2	178	0.52	0.78	33	GOL
3	210	0.50	0.76	31	empty
4	65	0.36	0.78	17	empty

Interfaces

1 interface between chains.

A–B · 544 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

2WEE · Crystal structure of Rv0371c from Mycobacterium tuberculosis H37Rv · 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 O53706
Elsewhere: RCSB PDB 2WEE · PDBe 2WEE · UniProt O53706

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