GL1X · GenesisL1 explorer

Research workbench

Structure of the ERS1 dimerization and histidine phosphotransfer domain from arabidopsis thaliana

Analyse Structure of the ERS1 dimerization and histidine phosphotransfer domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MTX
Type
protein
Length
384 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ethylene response sensor 1
EC
2.7.11.-, 2.7.13.3
UniProt
Q38846
Pockets
1 · best druggability 0.35

Structure

x-ray diffraction · 3 distinct chains · 90% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BEthylene response sensor 1 (EC 2.7.11.-, 2.7.13.3)protein9690% helix, 0% strandQ38846
CEthylene response sensor 1 (EC 2.7.11.-, 2.7.13.3)protein9789% helix, 0% strandQ38846
DEthylene response sensor 1 (EC 2.7.11.-, 2.7.13.3)protein9591% helix, 0% strandQ38846

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1670.350.7715empty

Interfaces

4 interfaces between chains.

  • C–D · 2174 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 2171 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 453 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 359 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 28 modified (engineered).

Compared structures

  • 4MTX · Structure of the ERS1 dimerization and histidine phosphotransfer domain from Arabidopsis… · the same entry in another collection · chain D against D, TM-score 1.00
  • Q38846 · AlphaFold monomer V2.0 prediction for ethylene response sensor 1 (Q38846) · a predicted model of the same protein · chain C against A, TM-score 0.92

Analyse

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