Research workbench

Ef-tu (escherichia COLI) in complex with nvp-LFF571

Analyse Ef-tu (escherichia COLI) in complex with nvp-LFF571 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3U2Q
Type: protein
Length: 396 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0CE47, Q7M0J8

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	385	—	P0CE47
B	—	protein	11	—	Q7M0J8

Compared structures

3U2Q · EF-Tu (Escherichia coli) in complex with NVP-LFF571 · the same entry in another collection · chain A against A, TM-score 1.00
P0CE47 · AlphaFold monomer V2.0 prediction for elongation factor tu 1 (P0CE47) · 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 P0CE47
Every structure of UniProt Q7M0J8
Elsewhere: RCSB PDB 3U2Q · PDBe 3U2Q · UniProt P0CE47 · UniProt Q7M0J8

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