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Crystal structure of aminotransferase from anaerococcus prevotii dsm 20548.

Analyse Crystal structure of aminotransferase from anaerococcus prevotii dsm 20548. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4EMY
Type
protein
Length
1,632 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aminotransferase class I and II
UniProt
C7REB0
Ligands
PLP
Pockets
17 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 46% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAminotransferase class I and IIprotein40947% helix, 15% strandC7REB0
CAminotransferase class I and IIprotein40743% helix, 16% strandC7REB0
DAminotransferase class I and IIprotein40746% helix, 16% strandC7REB0

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D

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

Pockets

17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110410.780.8086PLP
210280.780.8081PLP
310490.770.7988PLP
49870.760.7981PLP
5960.670.9122empty

Interfaces

3 interfaces between chains.

  • C–D · 3187 Ų buried · 45 hydrogen bonds · protein-protein
  • A–B · 3177 Ų buried · 48 hydrogen bonds · protein-protein
  • A–D · 197 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

  • 4EMY · Crystal structure of aminotransferase from anaerococcus prevotii dsm 20548. · the same entry in another collection · chain A against A, TM-score 1.00

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