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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: 7ED1
Type: protein
Length: 446 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4'-phosphopantetheinyl transferase
UniProt: A0A0D6HXZ9
Ligands: COA, CA
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	4'-phosphopantetheinyl transferase	protein	223	31% helix, 30% strand	A0A0D6HXZ9

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 6 copies · chains A, B
1PE · Pentaethylene glycol · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	618	0.76	0.82	65	COA, CA
2	432	0.71	0.81	41	COA, CA
3	174	0.61	0.83	28	empty
4	55	0.27	0.73	19	empty

Interfaces

1 interface between chains.

A–B · 823 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

7ED1 · 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 7ED1 · PDBe 7ED1 · UniProt A0A0D6HXZ9

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