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Crystal structure of enoyl-acyl carrier protein reductase (fabi) from neisseria meningitidis

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

PDB: 4M86
Type: protein
Length: 499 residues
Chains: 2
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: A1KVU8
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9)	protein	249	49% helix, 14% strand	A1KVU8
B	Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9)	protein	250	50% helix, 14% strand	A1KVU8

Pockets

3 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	626	0.71	0.78	49	empty
2	678	0.70	0.77	56	empty
3	192	0.48	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 1335 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4M86 · Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt A1KVU8
Elsewhere: RCSB PDB 4M86 · PDBe 4M86 · UniProt A1KVU8

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