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Crystal structure of eoyl-acp reductase with NADH

Analyse Crystal structure of eoyl-acp reductase with NADH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V35
Type: protein
Length: 574 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-acp reductase
EC: 1.3.1.9
UniProt: Q6LFB9
Ligands: NAI
Pockets: 6 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Enoyl-acp reductase (EC 1.3.1.9)	protein	287	48% helix, 17% strand	Q6LFB9

Ligands and binding sites

NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	518	0.81	0.87	47	NAI
2	517	0.80	0.87	45	NAI
3	201	0.58	0.80	25	empty
4	199	0.58	0.80	25	empty
5	281	0.54	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 1645 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

1V35 · Crystal Structure of Eoyl-ACP Reductase with NADH · 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 Q6LFB9
Elsewhere: RCSB PDB 1V35 · PDBe 1V35 · UniProt Q6LFB9

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