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Rifampin phosphotransferase G527Y mutant in complex with amppnp from listeria monocytogenes

Analyse Rifampin phosphotransferase G527Y mutant in complex with amppnp from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HV3
Type: protein
Length: 846 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoenolpyruvate synthase
UniProt: A0A0S2YLC8
Ligands: ANP, MG
Pockets: 9 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoenolpyruvate synthase	protein	846	44% helix, 15% strand	A0A0S2YLC8

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · 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

9 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	787	0.82	0.85	79	ANP, MG
2	410	0.57	0.74	38	empty
3	121	0.50	0.80	17	empty
4	211	0.48	0.75	32	empty
5	84	0.46	0.81	24	empty

Compared structures

5HV3 · Rifampin phosphotransferase G527Y mutant in complex with AMPPNP 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 5HV3 · PDBe 5HV3 · UniProt A0A0S2YLC8

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