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Crystal structure of human L-ARGININE:GLYCINE amidinotransferase in complex with alpha-amino butyric acid

Analyse Crystal structure of human L-ARGININE:GLYCINE amidinotransferase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 9JDW
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (L-ARGININE:GLYCINE amidinotransferase)
EC: 2.1.4.1
UniProt: P50440
Ligands: ABA
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (L-ARGININE:GLYCINE amidinotransferase) (EC 2.1.4.1)	protein	360	29% helix, 23% strand	P50440

Ligands and binding sites

ABA · Alpha-aminobutyric acid · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	236	0.66	0.84	45	ABA

Compared structures

9JDW · Crystal structure of human L-ARGININE:GLYCINE amidinotransferase in complex with… · 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 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P50440
Elsewhere: RCSB PDB 9JDW · PDBe 9JDW · UniProt P50440

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