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Crystal structure of E COLI enoyl reductase-NAD+-triclosan complex

Analyse Crystal structure of E COLI enoyl reductase-NAD+-triclosan complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1C14
Type: protein
Length: 512 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl reductase
EC: 1.3.1.9
UniProt: P29132
Ligands: NAD, TCL
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Enoyl reductase (EC 1.3.1.9)	protein	256	48% helix, 16% strand	P29132

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
TCL · Triclosan · ligand · 2 copies · chains A, B

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

Pockets

5 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	496	0.79	0.86	43	NAD, TCL
2	505	0.79	0.86	48	NAD, TCL
3	76	0.36	0.77	14	empty
4	68	0.31	0.74	16	empty
5	59	0.30	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 1697 Å² buried · 43 hydrogen bonds · protein-protein

Compared structures

1C14 · Crystal structure of E COLI enoyl reductase-NAD+-triclosan complex · 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 P29132
Elsewhere: RCSB PDB 1C14 · PDBe 1C14 · UniProt P29132

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