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Rifampin phosphotransferase in complex with amppnp and rifampin from listeria monocytogenes

Analyse Rifampin phosphotransferase in complex with amppnp and rifampin from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HV1
Type: protein
Length: 847 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoenolpyruvate synthase
UniProt: A0A0S2YLC8
Ligands: ANP, RFP, MG
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoenolpyruvate synthase	protein	847	47% helix, 15% strand	A0A0S2YLC8

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
RFP · Rifampicin · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

7 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	645	0.75	0.81	83	ANP, MG
2	809	0.71	0.76	60	RFP
3	349	0.59	0.77	42	empty
4	151	0.49	0.78	37	empty
5	151	0.47	0.77	24	empty

Compared structures

5HV1 · Rifampin phosphotransferase in complex with AMPPNP and rifampin from Listeria… · 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 5HV1 · PDBe 5HV1 · UniProt A0A0S2YLC8

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