Research workbench

Ef-tu complexed with a GTP analog and the antibiotic pulvomycin

Analyse Ef-tu complexed with a GTP analog and the antibiotic pulvomycin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C78
Type: protein
Length: 397 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q5SHN6

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	397	—	Q5SHN6

Compared structures

2C78 · EF-Tu complexed with a GTP analog and the antibiotic pulvomycin · the same entry in another collection · chain A against A, TM-score 1.00
Q5SHN6 · AlphaFold monomer V2.0 prediction for elongation factor tu-a (Q5SHN6) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 Q5SHN6
Elsewhere: RCSB PDB 2C78 · PDBe 2C78 · UniProt Q5SHN6

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