MolNFT v1 · #12859 · protein

Crystal structure of elongation factor G dimer without nucleotide

1KTV: “Crystal structure of elongation factor G dimer without nucleotide”. X-ray diffraction, 16 pockets (best druggability 0.77). MolNFT v1 #12859 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1KTV
Type: protein
Length: 1,264 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor G
UniProt: P13551
Pockets: 16 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Elongation factor G	protein	632	24% helix, 27% strand	P13551

Pockets

16 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	927	0.77	0.79	94	empty
2	751	0.76	0.81	67	empty
3	465	0.62	0.76	46	empty
4	300	0.59	0.78	36	empty
5	185	0.56	0.80	26	empty

Interfaces

1 interface between chains.

A–B · 858 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1KTV · Crystal Structure of Elongation Factor G Dimer Without Nucleotide · 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 B against A, TM-score 0.76

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 1KTV · PDBe 1KTV · UniProt P13551

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