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Lipid transfer protein complexed with palmitoyl coenzyme a, NMR, 16 structures

Analyse Lipid transfer protein complexed with palmitoyl coenzyme a, NMR, 16 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JTB
Type: protein
Length: 91 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipid transfer protein
UniProt: P07597
Ligands: COA, PLM
Pockets: 1 · best druggability 0.79

Structure

solution nmr · 1 distinct chain · 55% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipid transfer protein	protein	91	55% helix, 0% strand	P07597

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
PLM · Palmitic acid · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	224	0.79	0.92	34	PLM

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1JTB · Lipid transfer protein complexed with palmitoyl coenzyme a, NMR, 16 structures · the same entry in another collection · chain A against A, TM-score 1.00
P07597 · AlphaFold monomer V2.0 prediction for non-specific lipid-transfer protein 1 (P07597) · a predicted model of the same protein · chain A against A, TM-score 0.72

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 P07597
Elsewhere: RCSB PDB 1JTB · PDBe 1JTB · UniProt P07597

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