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The crystal structure of fabv

Analyse The crystal structure of fabv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S8M
Type: protein
Length: 390 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-acp reductase
EC: 1.3.1.-
UniProt: Q2P9J6
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-acp reductase (EC 1.3.1.-)	protein	390	45% helix, 17% strand	Q2P9J6

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	767	0.79	0.83	70	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

3S8M · The Crystal Structure of FabV · the same entry in another collection · chain A against A, TM-score 1.00
Q2P9J6 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH]… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q2P9J6
Elsewhere: RCSB PDB 3S8M · PDBe 3S8M · UniProt Q2P9J6

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