› 5gv2

X-ray diffraction
2.06Å resolution

Crystal structure of Arginine-bound CASTOR1 from Homo sapiens

Released:
DOI: 10.2210/pdb5gv2/pdb
PDB entry 5gv2 coloured by chain, front view.
PDB entry 5gv2 coloured by chain, side view.
PDB entry 5gv2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural mechanism for the arginine sensing and regulation of CASTOR1 in the mTORC1 signaling pathway.
Gai Z, Wang Q, Yang C, Wang L, Deng W, Wu G
Cell Discov 2 16051 (2016)
PMID: 28066558

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosolic arginine sensor for mTORC1 subunit 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 349 amino acids
Theoretical weight: 38.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WTX7 (Residues: 1-329; Coverage: 100%)
Gene names: CASTOR1, GATSL3
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ARG 1 x ARG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P21
Unit cell:
a: 47.547Å b: 76.834Å c: 95.223Å
α: 90° β: 96.21° γ: 90°
R-values:
R R work R free
0.192 0.19 0.238
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Amino acid-dependent control of mTORC1 signaling: a variety of regulatory modes.
Takahara et al. (2020)
9 more

1 mention without citation

Structural mechanism for the arginine sensing and regulation of CASTOR1 in the mTORC1 signaling pathway.
Gai et al. (2016)