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Crystal structure of maf domain of human N-acetylserotonin O- methyltransferase-like protein

Analyse Crystal structure of maf domain of human N-acetylserotonin O… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2P5X
Type
protein
Length
405 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-acetylserotonin O-methyltransferase-like protein
UniProt
O95671
Ligands
PO4
Pockets
5 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AN-acetylserotonin O-methyltransferase-like proteinprotein20442% helix, 28% strandO95671
BN-acetylserotonin O-methyltransferase-like proteinprotein20137% helix, 26% strandO95671

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13390.620.7843PO4
22300.520.7624empty
31090.480.8122PO4
4750.430.8119empty
51070.380.7421empty

Interfaces

1 interface between chains.

  • A–B · 919 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 2P5X · Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like… · the same entry in another collection · chain A against A, TM-score 1.00
  • O95671 · AlphaFold monomer V2.0 prediction for probable bifunctional DTTP/UTP… · a predicted model of the same protein · chain A against A, TM-score 0.99

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