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The ATP binding domain of rifampin phosphotransferase from listeria monocytogenes

Analyse The ATP binding domain of rifampin phosphotransferase from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HV6
Type: protein
Length: 599 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoenolpyruvate synthase
UniProt: A0A0S2YLC8
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoenolpyruvate synthase	protein	308	36% helix, 23% strand	A0A0S2YLC8
B	Phosphoenolpyruvate synthase	protein	291	34% helix, 23% strand	A0A0S2YLC8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.72	0.97	18	empty
2	83	0.70	0.94	24	empty
3	402	0.64	0.78	37	empty
4	434	0.61	0.76	43	empty
5	153	0.46	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 1091 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

5HV6 · The ATP binding domain of rifampin phosphotransferase from Listeria monocytogenes · 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 A0A0S2YLC8
Elsewhere: RCSB PDB 5HV6 · PDBe 5HV6 · UniProt A0A0S2YLC8

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