MolNFT v1 · #32295 · protein

Ribosomal elongation factor G (ef-G) fusidic acid resistant mutant G16V

2BM1: “Ribosomal elongation factor G (ef-G) fusidic acid resistant mutant G16V”. X-ray diffraction, 2 ligands (GDP, MG), 7 pockets (best druggability 0.78). MolNFT v1 #32295 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2BM1
Type: protein
Length: 660 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor G
UniProt: P13551
Ligands: GDP, MG
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor G	protein	660	26% helix, 32% strand	P13551

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	957	0.78	0.80	96	empty
2	150	0.58	0.83	31	MG
3	219	0.50	0.76	34	empty
4	53	0.49	0.86	18	empty
5	89	0.41	0.78	26	empty

Compared structures

2BM1 · Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant G16V · the same entry in another collection · chain A against A, TM-score 1.00
P13551 · AlphaFold monomer V2.0 prediction for elongation factor G (P13551) · a predicted model of the same protein · chain A against A, TM-score 0.71

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 P13551
Elsewhere: RCSB PDB 2BM1 · PDBe 2BM1 · UniProt P13551

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