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Crystal structure of RV3119 from mycobacterium tuberculosis

Analyse Crystal structure of RV3119 from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WP4
Type: protein
Length: 253 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Molybdopterin-converting factor subunit 2 1
UniProt: O05795
Ligands: CA
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Molybdopterin-converting factor subunit 2 1	protein	121	35% helix, 34% strand	O05795
B	Molybdopterin-converting factor subunit 2 1	protein	132	33% helix, 36% strand	O05795

Ligands and binding sites

CA · Calcium ion · metal · chains B
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	253	0.61	0.80	24	empty
2	183	0.49	0.76	29	empty
3	50	0.26	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 1282 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2WP4 · crystal structure of Rv3119 from Mycobacterium 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 O05795
Elsewhere: RCSB PDB 2WP4 · PDBe 2WP4 · UniProt O05795

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