Research workbench
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
- 4JDW
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50440
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 361 | — | P50440 |
Compared structures
- 4JDW · 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 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 4JDW · PDBe 4JDW · UniProt P50440
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