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Crystal structure of glutamate-1-semialdehyde 2,1- aminomutase from aeropyrum pernix

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

PDB
2ZSL
Type
protein
Length
420 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
Q9Y9I9
Ligands
PMP
Pockets
6 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8)protein42045% helix, 18% strandQ9Y9I9

Ligands and binding sites

  • PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.751.0015empty
23400.580.7646PMP
31930.490.7523empty
41270.440.7730empty
5910.390.7718empty

Compared structures

  • 2ZSL · Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from Aeropyrum pernix · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y9I9 · AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase (Q9Y9I9) · a predicted model of the same protein · chain A against A, TM-score 1.00

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