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NMR solution structures of 3-oxooctanyl-acp from streptomyces coelicolor fatty acid synthase

Analyse NMR solution structures of 3-oxooctanyl-acp from streptomyces coelicolor fatty… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KOP
Type: protein
Length: 81 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl carrier protein
UniProt: P72393
Ligands: SYO
Pockets: 1 · best druggability 0.44

Structure

solution nmr · 1 distinct chain · 57% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acyl carrier protein	protein	81	57% helix, 0% strand	P72393

Ligands and binding sites

SYO · [(3S)-3-hydroxy-2,2-dimethyl-4-oxo-4-[[3-oxo-3-[2-(3-oxooctylsulfanyl)ethylamino]propyl]amino]butyl] dihydrogen phosphate · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.44	0.82	18	SYO

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2KOP · NMR solution structures of 3-oxooctanyl-ACP from Streptomyces coelicolor Fatty Acid… · 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 P72393
Elsewhere: RCSB PDB 2KOP · PDBe 2KOP · UniProt P72393

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