Research workbench

Structure of phosphorylated ef-tu in complex with GTP

Analyse Structure of phosphorylated ef-tu in complex with GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OPD
Type: protein
Length: 756 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: A8A5E6
Ligands: GTP, NA, MG, IOD

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	377	—	A8A5E6
B	—	protein	379	—	A8A5E6

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · 5 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
IOD · Iodide ion · ion · 28 copies · chains A, B
GOL · Glycerol · additive · chains A

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

Compared structures

5OPD · Structure of phosphorylated EF-Tu in complex with GTP · the same entry in another collection · chain A against A, TM-score 1.00
A8A5E6 · AlphaFold monomer V2.0 prediction for elongation factor tu 1 (A8A5E6) · a predicted model of the same protein · chain A 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 5OPD · PDBe 5OPD · UniProt A8A5E6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.