MolNFT v1 · #104412 · protein

Crystal structure of chlamydia trachomatis enoyl-acp reductase (fabi) in complex with NADH and afn-1252

4Q9N · Enoyl-[acyl-carrier-protein] reductase [NADH]: “Crystal structure of chlamydia trachomatis enoyl-acp reductase (fabi) in complex with NADH and afn-1252”. X-ray diffraction, 2 ligands (NAI, 0WE), 13 pockets (best druggability 0.84).…

PDB: 4Q9N
Type: protein
Length: 2,360 residues
Chains: 8
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: T1TQB5
Ligands: NAI, 0WE
Pockets: 13 · best druggability 0.84

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9)	protein	295	48% helix, 17% strand	T1TQB5

Ligands and binding sites

NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
0WE · N-methyl-N-[(3-methyl-1-benzofuran-2-yl)methyl]-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) propanamide · ligand · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1086	0.84	0.86	48	empty
2	1196	0.84	0.85	48	empty
3	432	0.83	0.91	48	NAI, 0WE
4	593	0.83	0.88	51	NAI, 0WE
5	396	0.82	0.91	49	NAI, 0WE

Interfaces

13 interfaces between chains.

G–H · 1807 Å² buried · 42 hydrogen bonds · protein-protein
E–F · 1795 Å² buried · 40 hydrogen bonds · protein-protein
A–B · 1792 Å² buried · 39 hydrogen bonds · protein-protein
E–H · 1784 Å² buried · 21 hydrogen bonds · protein-protein
B–C · 1779 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

4Q9N · Crystal structure of Chlamydia trachomatis enoyl-ACP reductase (FabI) in complex with… · the same entry in another collection · chain B against B, 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 T1TQB5
Elsewhere: RCSB PDB 4Q9N · PDBe 4Q9N · UniProt T1TQB5

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