MolNFT v1 · #53937 · protein

Structure of the mycobacterium tuberculosis protein, RV2275, demonstrates that cyclodipeptide synthetases are related to type I tRNA-synthetases.

2X9Q: “Structure of the mycobacterium tuberculosis protein, RV2275, demonstrates that cyclodipeptide synthetases are…”. X-ray diffraction, 5 pockets (best druggability 0.66). MolNFT v1 #53937 on GenesisL1: 3D structure, binding sites and…

PDB: 2X9Q
Type: protein
Length: 453 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclodipeptide synthetase
UniProt: Q50688
Pockets: 5 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclodipeptide synthetase	protein	231	54% helix, 16% strand	Q50688
B	Cyclodipeptide synthetase	protein	222	53% helix, 17% strand	Q50688

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	333	0.66	0.81	38	empty
2	424	0.66	0.79	32	empty
3	241	0.61	0.80	31	empty
4	149	0.56	0.82	28	empty
5	62	0.31	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 1174 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2X9Q · Structure of the Mycobacterium tuberculosis protein, Rv2275, demonstrates that… · 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 Q50688
Elsewhere: RCSB PDB 2X9Q · PDBe 2X9Q · UniProt Q50688

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