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Whole, unmodified, ef-TU(ELONGATION factor tu).

Analyse Whole, unmodified, ef-TU(ELONGATION factor tu). in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DG1
Type: protein
Length: 770 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor tu
UniProt: P0A6N1
Ligands: GDP, MG
Pockets: 5 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
G, H	Elongation factor tu	protein	385	25% helix, 39% strand	P0A6N1

Ligands and binding sites

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

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

Pockets

5 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	260	0.50	0.74	36	empty
2	91	0.45	0.80	21	empty
3	157	0.42	0.74	26	empty
4	113	0.38	0.75	18	empty
5	64	0.30	0.74	20	MG, GDP

Interfaces

1 interface between chains.

G–H · 473 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1DG1 · Whole, unmodified, ef-TU(ELONGATION factor tu). · the same entry in another collection · chain G against G, 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 1DG1 · PDBe 1DG1 · UniProt P0A6N1

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