› 5eog

X-ray diffraction
3.05Å resolution

Structure of full-length human MAB21L1

Released:
DOI: 10.2210/pdb5eog/pdb
PDB entry 5eog coloured by chain, front view.
PDB entry 5eog coloured by chain, side view.
PDB entry 5eog coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical characterization of the cell fate determining nucleotidyltransferase fold protein MAB21L1.
de Oliveira Mann CC, Kiefersauer R, Witte G, Hopfner KP
Sci Rep 6 27498 (2016)
PMID: 27271801

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative nucleotidyltransferase MAB21L1 Chains: A, B, C, D, F
Molecule details ›
Chains: A, B, C, D, F
Length: 362 amino acids
Theoretical weight: 41.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13394 (Residues: 2-359; Coverage: 100%)
Gene names: CAGR1, MAB21L1, Nbla00126
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand CIT 5 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 167.1Å b: 176.99Å c: 115.11Å
α: 90° β: 126.53° γ: 90°
R-values:
R R work R free
0.225 0.223 0.28
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Evolutionary Origins of cGAS-STING Signaling.
Margolis et al. (2017)
6 more

2 mentions without citation

Structural and biochemical characterization of the cell fate determining nucleotidyltransferase fold protein MAB21L1.
de Oliveira Mann et al. (2016)
1 more