MolNFT v1 · #183584 · protein

Cryo-EM structure of the mycolic acid transporter MMPL3 from M. tuberculosis

7NVH · Trehalose monomycolate rnd transporter MMPL3: “Cryo-EM structure of the mycolic acid transporter MMPL3 from M. tuberculosis”. Electron microscopy, 1 ligand (AV0), 4 pockets (best druggability 0.76). MolNFT v1 #183584 on GenesisL1…

PDB: 7NVH
Type: protein
Length: 717 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trehalose monomycolate rnd transporter MMPL3
UniProt: A0A658HT16
Ligands: AV0
Pockets: 4 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 62% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trehalose monomycolate rnd transporter MMPL3	protein	717	62% helix, 7% strand	A0A658HT16

Ligands and binding sites

AV0 · 2-decyl-2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}dodecyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside · ligand · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1194	0.76	0.78	87	AV0
2	87	0.74	0.96	26	empty
3	149	0.42	0.75	29	empty
4	75	0.36	0.75	19	empty

Compared structures

7NVH · Cryo-EM structure of the mycolic acid transporter MmpL3 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 A0A658HT16
Elsewhere: RCSB PDB 7NVH · PDBe 7NVH · UniProt A0A658HT16

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