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Phosphopantetheine adenylyltransferase from mycobacterium tuberculosis in complex with 3-(1H-indol-3-YL)PROPANOIC acid at 1.6A resolution.

Analyse Phosphopantetheine adenylyltransferase from mycobacterium tuberculosis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G7T
Type: protein
Length: 152 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphopantetheine adenylyltransferase
EC: 2.7.7.3
UniProt: P9WPA5
Ligands: IOP
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphopantetheine adenylyltransferase (EC 2.7.7.3)	protein	152	47% helix, 20% strand	P9WPA5

Ligands and binding sites

IOP · Indolylpropionic 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	293	0.63	0.80	38	IOP
2	74	0.37	0.77	15	empty

Compared structures

P9WPA5 · AlphaFold monomer V2.0 prediction for phosphopantetheine adenylyltransferase (P9WPA5) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P9WPA5
Elsewhere: RCSB PDB 6G7T · PDBe 6G7T · UniProt P9WPA5

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