4DYO

Crystal Structure of Human Aspartyl Aminopeptidase (DNPEP) in complex with Aspartic acid Hydroxamate

Replaces:  3L6S

Summary for 4DYO

• Entry DOI: 10.2210/pdb4dyo/pdb
• Descriptor: Aspartyl aminopeptidase, ZINC ION, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: structural genomics, structural genomics consortium, sgc, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9ULA0
• Total number of polymer chains: 1
• Total formula weight: 54421.16

Authors

Chaikuad, A.,Pilka, E.,Vollmar, M.,Krojer, T.,Muniz, J.R.C.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Weigelt, J.,Bountra, C.,Kavanagh, K.L.,Oppermann, U.,Structural Genomics Consortium (SGC) (deposition date: 2012-02-29, release date: 2012-03-14, Last modification date: 2023-12-06)

Primary citation

Chaikuad, A.,Pilka, E.S.,Riso, A.D.,Delft, F.V.,Kavanagh, K.L.,Venien-Bryan, C.,Oppermann, U.,Yue, W.W.
Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
Bmc Struct.Biol., 12:14-14, 2012

PubMed Abstract: Aspartyl aminopeptidase (DNPEP), with specificity towards an acidic amino acid at the N-terminus, is the only mammalian member among the poorly understood M18 peptidases. DNPEP has implicated roles in protein and peptide metabolism, as well as the renin-angiotensin system in blood pressure regulation. Despite previous enzyme and substrate characterization, structural details of DNPEP regarding ligand recognition and catalytic mechanism remain to be delineated.

PubMed: 22720794
DOI: 10.1186/1472-6807-12-14

Experimental method

X-RAY DIFFRACTION (2.2 Å)