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EBI PDBe PDBeView

PDBe Entry: 1pqu view

Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae Bound with NADP, S-methyl cysteine sulfoxide and cacodylate
Summary
Header OXIDOREDUCTASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.92 Å, R-factor: 18.4%, Free R-factor: 23.4%, Spacegroup: P 1 21 1
Released 10/08/2004, deposition: 19/06/2003, last revision: 24/02/2009
Authors Blanco, J.search; Moore, R.A.search; Viola, R.E.search
Primary citation The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
ACTA CRYSTALLOGR.,SECT.Dsearch vol:60, pag:1388-1395 (2004) [PubMed ID 15272161 ]search
Keywords Enzymesearch, L-aspartate semialdehydesearch, cacodylatesearch, NADPsearch, OXIDOREDUCTASEsearch
EC 1.2.1.11 ExPASy BRENDA search (A B C D)
Organism Haemophilus influenzae Rd KW20 71421search(A B C D)
UniProt Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) (ASA dehydrogenase) (ASADH) P44801search (A B C D)
Solvent A, B, C, D
Related entries 1nwc, 1nwh, 1nx6, 1pqp, 1pr3, 1ps8, 1pu2
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D Aspartate-semialdehyde dehydrogenase Protein P44801 (DHAS_HAEIN)search
 371 100%
Heterogens
Id Name Ligands
A, B, C, D CACODYLATE ION CAC search
A, B, D NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE NAP search
A, B, C, D CYSTEINE CYS search
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