MolNFT v1 · #126949 · protein

Structure of the phosphomimetic mutant of ef-tu T383E

5MI8: “Structure of the phosphomimetic mutant of ef-tu T383E”. X-ray diffraction, 3 ligands (GDP, MG, CL). MolNFT v1 #126949 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5MI8
Type: protein
Length: 769 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: A8A5E6
Ligands: GDP, MG, CL

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	386	—	A8A5E6
B	—	protein	383	—	A8A5E6

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B
CL · Chloride ion · ion · chains B
ACT · Acetate ion · additive · 4 copies · chains A, B
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B

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

Compared structures

5MI8 · Structure of the phosphomimetic mutant of EF-Tu T383E · the same entry in another collection · chain B against B, TM-score 1.00
A8A5E6 · AlphaFold monomer V2.0 prediction for elongation factor tu 1 (A8A5E6) · a predicted model of the same protein · chain B against A, TM-score 0.59

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 A8A5E6
Elsewhere: RCSB PDB 5MI8 · PDBe 5MI8 · UniProt A8A5E6

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