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Crystal structure of SCO1815: a beta-ketoacyl-acyl carrier protein reductase from streptomyces coelicolor A3(2)

Analyse Crystal structure of SCO1815: a beta-ketoacyl-acyl carrier protein reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NM0
Type
protein
Length
442 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable 3-oxacyl-(acyl-carrier-protein) reductase
EC
1.1.1.100
UniProt
Q9S274
Pockets
3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProbable 3-oxacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100)protein22143% helix, 18% strandQ9S274

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14140.730.8354empty
24670.660.7877empty
31530.640.8724empty

Interfaces

1 interface between chains.

  • A–B · 1494 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 2NM0 · Crystal Structure of SCO1815: a Beta-Ketoacyl-Acyl Carrier Protein Reductase from… · the same entry in another collection · chain A against A, TM-score 1.00

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