MolNFT v1 · #5352 · protein

Intact elongation factor from E.COLI

1EFC · Protein (elongation factor): “Intact elongation factor from E.COLI”. X-ray diffraction, 2 ligands (GDP, MG), 6 pockets (best druggability 0.62). MolNFT v1 #5352 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1EFC
Type: protein
Length: 772 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (elongation factor)
UniProt: P0A6N1
Ligands: GDP, MG
Pockets: 6 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein (elongation factor)	protein	386	24% helix, 38% strand	P0A6N1

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

6 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	421	0.62	0.77	53	empty
2	185	0.51	0.78	42	empty
3	174	0.46	0.75	24	empty
4	85	0.43	0.79	20	empty
5	74	0.34	0.75	20	MG, GDP

Interfaces

1 interface between chains.

A–B · 521 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1EFC · Intact elongation factor from E.COLI · 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 P0A6N1
Elsewhere: RCSB PDB 1EFC · PDBe 1EFC · UniProt P0A6N1

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