MolNFT v1 · #156900 · protein

Crystal structure of ef-tu from acinetobacter baumannii in complex with MG2+ and GDP

6MIJ · Elongation factor tu: “Crystal structure of ef-tu from acinetobacter baumannii in complex with MG2+ and GDP”. X-ray diffraction, 2 ligands (GDP, MG), 4 pockets (best druggability 0.47). MolNFT v1 #156900 on GenesisL1: 3D structure…

PDB: 6MIJ
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor tu
UniProt: N9JNN0
Ligands: GDP, MG
Pockets: 4 · best druggability 0.47

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor tu	protein	388	24% helix, 38% strand	N9JNN0

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
FMT · Formic acid · additive · 8 copies · chains A

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

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	163	0.47	0.76	28	FMT
2	88	0.38	0.76	22	empty
3	89	0.37	0.76	26	MG, GDP
4	63	0.32	0.75	15	empty

Compared structures

6MIJ · Crystal structure of EF-Tu from Acinetobacter baumannii in complex with Mg2+ and GDP · 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 N9JNN0
Elsewhere: RCSB PDB 6MIJ · PDBe 6MIJ · UniProt N9JNN0

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