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Crystal structure and mechanism of L-arginine: glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis

Analyse Crystal structure and mechanism of L-arginine: glycine amidinotransferase: a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1JDW
Type
protein
Length
360 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-ARGININE\:GLYCINE amidinotransferase
EC
2.1.4.1
UniProt
P50440
Pockets
2 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-ARGININE\:GLYCINE amidinotransferase (EC 2.1.4.1)protein36029% helix, 24% strandP50440

Ligands and binding sites

  • BME · Beta-mercaptoethanol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11080.380.7522empty
2500.320.7716empty

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

  • 1JDW · Crystal structure and mechanism of L-arginine: glycine amidinotransferase: a… · the same entry in another collection · chain A against A, TM-score 1.00
  • P50440 · AlphaFold monomer V2.0 prediction for glycine amidinotransferase, mitochondrial (P50440) · a predicted model of the same protein · chain A against A, TM-score 1.00

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