MolNFT v1 · #31286 · protein

Crystal structure of wild-type of enoyl-ACP(COA) reductase from mycobacterium tuberculosis in complex with NADH.

2AQ8 · Enoyl-acyl-carrier-protein reductase: “Crystal structure of wild-type of enoyl-ACP(COA) reductase from mycobacterium tuberculosis in complex with…”. X-ray diffraction, 2 ligands (NAI, LYS), 2 pockets (best druggability 0.78). MolNFT…

PDB: 2AQ8
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-acyl-carrier-protein reductase
EC: 1.3.1.9
UniProt: P0A5Y6
Ligands: NAI, LYS
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-acyl-carrier-protein reductase (EC 1.3.1.9)	protein	267	47% helix, 16% strand	P0A5Y6

Ligands and binding sites

NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains A
LYS · Lysine · ligand · chains A

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

Pockets

2 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	652	0.78	0.83	47	NAI
2	75	0.36	0.77	16	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2AQ8 · Crystal structure of wild-type of Enoyl-ACP(CoA) reductase from Mycobacterium… · 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 P0A5Y6
Elsewhere: RCSB PDB 2AQ8 · PDBe 2AQ8 · UniProt P0A5Y6

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