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Crystal structure of human pyridoxal phosphate phosphatase with MG2+ at 1.9 a resolution

Analyse Crystal structure of human pyridoxal phosphate phosphatase with MG2+ at 1.9 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2P27
Type
protein
Length
289 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pyridoxal phosphate phosphatase
EC
3.1.3.74
UniProt
Q96GD0
Ligands
MG
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APyridoxal phosphate phosphatase (EC 3.1.3.74)protein28942% helix, 20% strandQ96GD0

Ligands and binding sites

  • MG · Magnesium ion · metal · 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
12990.720.8536empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 2P27 · Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Mg2+ at 1.9 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96GD0 · AlphaFold monomer V2.0 prediction for pyridoxal phosphate phosphatase (Q96GD0) · a predicted model of the same protein · chain A against A, TM-score 0.98

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