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Transferase from mycobacterium tuberculosis

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

PDB: 7ED2
Type: protein
Length: 442 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4'-phosphopantetheinyl transferase
UniProt: A0A0D6HXZ9
Ligands: A3P, MG
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	4'-phosphopantetheinyl transferase	protein	221	32% helix, 31% strand	A0A0D6HXZ9

Ligands and binding sites

A3P · Adenosine-3'-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B

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	1025	0.80	0.81	101	A3P, MG
2	155	0.61	0.84	34	empty

Interfaces

1 interface between chains.

A–B · 793 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

7ED2 · Transferase from Mycobacterium smegmatis · 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 A0A0D6HXZ9
Elsewhere: RCSB PDB 7ED2 · PDBe 7ED2 · UniProt A0A0D6HXZ9

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