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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: 2JDW
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: 1 · best druggability 0.40

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-ARGININE\:GLYCINE amidinotransferase (EC 2.1.4.1)	protein	360	29% helix, 24% strand	P50440

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.40	0.76	21	empty

Compared structures

2JDW · 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

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 2JDW · PDBe 2JDW · UniProt P50440

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