MolNFT v1 · #14659 · protein

Hypothetical protein TM841 from thermotoga maritima reveals fatty acid binding function

1MGP: “Hypothetical protein TM841 from thermotoga maritima reveals fatty acid binding function”. X-ray diffraction, 1 ligand (PLM), 2 pockets (best druggability 0.75). MolNFT v1 #14659 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1MGP
Type: protein
Length: 276 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TM841
UniProt: Q9X1H9
Ligands: PLM
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TM841	protein	276	39% helix, 28% strand	Q9X1H9

Ligands and binding sites

PLM · Palmitic acid · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.75	0.95	30	PLM
2	212	0.61	0.82	28	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

1MGP · Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function · the same entry in another collection · chain A against A, TM-score 1.00
Q9X1H9 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein TM_1468 (Q9X1H9) · 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 Q9X1H9
Elsewhere: RCSB PDB 1MGP · PDBe 1MGP · UniProt Q9X1H9

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