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Fatty acid ABC transporter substrate-binding protein from thermomonospora curvata

Analyse Fatty acid ABC transporter substrate-binding protein from thermomonospora… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N03
Type: protein
Length: 389 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC-type branched-chain amino acid transport systems periplasmic component-like protein
UniProt: D1A9M1
Ligands: PLM
Pockets: 1 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC-type branched-chain amino acid transport systems periplasmic component-like protein	protein	389	41% helix, 20% strand	D1A9M1

Ligands and binding sites

PLM · Palmitic acid · ligand · chains A
EDO · 1,2-ethanediol · additive · 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	239	0.84	0.96	49	PLM

Modifications

Observed in the structure: 8 modified, 1 disulfide (engineered, disulfide).

Compared structures

4N03 · Fatty acid ABC transporter substrate-binding protein from Thermomonospora curvata · 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 D1A9M1
Elsewhere: RCSB PDB 4N03 · PDBe 4N03 · UniProt D1A9M1

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