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Crystal structure of moraxella catarrhalis enoyl-acp-reductase (fabi) in complex with the cofactor NAD

Analyse Crystal structure of moraxella catarrhalis enoyl-acp-reductase (fabi) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F44
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 [NADH]
EC: 1.3.1.9
UniProt: D5VCE0
Ligands: NAD, CA
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9)	protein	267	51% helix, 13% strand	D5VCE0

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
CA · Calcium ion · metal · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	736	0.72	0.78	52	NAD, GOL

Compared structures

7F44 · Crystal structure of Moraxella catarrhalis enoyl-ACP-reductase (FabI) in complex with the… · 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 D5VCE0
Elsewhere: RCSB PDB 7F44 · PDBe 7F44 · UniProt D5VCE0

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