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Structure of an amidohydrolase from chromobacterium violaceum (efi target efi-500202) with bound mn, AMP and phosphate.

Analyse Structure of an amidohydrolase from chromobacterium violaceum (efi target… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YB1
Type
protein
Length
284 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Amidohydrolase
UniProt
Q7NXD4
Ligands
AMP, MN, PO4
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAmidohydrolaseprotein28442% helix, 16% strandQ7NXD4

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · chains A
  • MN · Manganese (II) ion · metal · 3 copies · chains A
  • PO4 · Phosphate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14060.650.7942MN, AMP, PO4

Compared structures

  • 2YB1 · Structure of an amidohydrolase from Chromobacterium violaceum (EFI target EFI-500202)… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q7NXD4 · AlphaFold monomer V2.0 prediction for 3',5'-nucleoside bisphosphate phosphatase (Q7NXD4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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