GL1X · GenesisL1 explorer

Research workbench

Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from stenotrophomonas maltophilia K279A in complex with plp

Analyse Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6W80
Type
protein
Length
430 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate-1-semialdehyde 2,1-aminomutase
EC
5.4.3.8
UniProt
B2FT35
Ligands
PLP
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8)protein43043% helix, 17% strandB2FT35

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16480.690.7765PLP
21110.370.7418empty
3740.320.7416empty

Compared structures

  • 6W80 · Crystal structure of Glutamate-1-semialdehyde 2,1-aminomutase from Stenotrophomonas… · the same entry in another collection · chain A against A, TM-score 1.00
  • B2FT35 · AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase (B2FT35) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

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