Crystal structure of the M180A mutant of the aminopeptidase from Vibrio proteolyticus

Summary for 3B35

Related3B3C 3B3S 3B3T 3B3V 3B3W
DescriptorBacterial leucyl aminopeptidase, ZINC ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsalpha beta, aminopeptidase, hydrolase, metal-binding, protease, secreted, zinc, zymogen
Biological sourceVibrio proteolyticus
Cellular locationSecreted Q01693
Total number of polymer chains1
Total molecular weight31775.14
Ataie, N.J.,Hoang, Q.Q.,Petsko, G.A.,Ringe, D. (deposition date: 2007-10-19, release date: 2007-11-27, Last modification date: 2011-07-13)
Primary citation
Ataie, N.J.,Hoang, Q.Q.,Zahniser, M.P.,Tu, Y.,Milne, A.,Petsko, G.A.,Ringe, D.
Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus.
Biochemistry, 47:7673-7683, 2008
PubMed: 18576673 (PDB entries with the same primary citation)
DOI: 10.1021/bi702188e
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.1656 0.3% 1.3% 3.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-10-28