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Phosphopantetheine adenylyltransferase from mycobacterium tuberculosis in complex with 3-(1H-indol-1-YL)PROPANOIC acid at 1.7A 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: 6G7S
Type: protein
Length: 151 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: EQ5
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphopantetheine adenylyltransferase (EC 2.7.7.3)	protein	151	46% helix, 19% strand	P9WPA5

Ligands and binding sites

EQ5 · 3-indol-1-ylpropanoic acid · ligand · chains A
DMS · Dimethyl sulfoxide · additive

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	280	0.64	0.81	36	EQ5

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

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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 6G7S · PDBe 6G7S · UniProt P9WPA5

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