Research workbench

Ef-TU.KIRROMYCIN coordinates fitted into the cryo-EM MAP of ef-tu ternary complex (GDP.KIRROMYCIN) bound 70S ribosome

Analyse Ef-TU.KIRROMYCIN coordinates fitted into the cryo-EM MAP of ef-tu ternary… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QZD
Type: protein
Length: 393 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor tu
UniProt: P0A6N1
Pockets: 4 · best druggability 0.42

Structure

electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor tu	protein	393	0% helix, 0% strand	P0A6N1

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	145	0.42	0.73	33	empty
2	90	0.35	0.72	25	empty
3	89	0.34	0.72	32	empty
4	51	0.27	0.72	16	empty

Compared structures

1QZD · EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex… · 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 1QZD · PDBe 1QZD · UniProt P0A6N1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.