PDBe 2evu

X-ray diffraction
2.3Å resolution

Crystal structure of aquaporin AqpM at 2.3A resolution

Released:
Primary publication:
Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A.
Proc. Natl. Acad. Sci. U.S.A. 102 18932-7 (2005)
PMID: 16361443

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin AqpM Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 25.36 KDa
Source organism: Methanothermobacter marburgensis str. Marburg
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9C4Z5 (Residues: 1-246; Coverage: 100%)
Gene names: MTBMA_c05510, aqpM
Sequence domains: Major intrinsic protein
Structure domains: Glycerol uptake facilitator protein.

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: I4
Unit cell:
a: 93.887Å b: 93.887Å c: 77.744Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.226
Expression system: Escherichia coli