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Brassica napus enoyl acp REDUCTASE/NAD binary complex at pH 8.0 and room temperature

Analyse Brassica napus enoyl acp REDUCTASE/NAD binary complex at pH 8.0 and room… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ENO
Type: protein
Length: 297 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: P80030
Ligands: NAD
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl acyl carrier protein reductase (EC 1.3.1.9)	protein	297	46% helix, 16% strand	P80030

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · 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	457	0.64	0.77	43	NAD
2	104	0.49	0.81	21	empty

Compared structures

1ENO · Brassica napus enoyl acp REDUCTASE/NAD binary complex at pH 8.0 and room temperature · the same entry in another collection · chain A against A, TM-score 1.00
P80030 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH]… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P80030
Elsewhere: RCSB PDB 1ENO · PDBe 1ENO · UniProt P80030

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