1PQP

Crystal Structure of the C136S Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae Bound with Aspartate Semialdehyde and Phosphate

Summary for 1PQP
Related1NWC 1NWH 1NX6
DescriptorAspartate-semialdehyde dehydrogenase, PHOSPHATE ION, L-HOMOSERINE, ... (4 entities in total)
Functional Keywordsenzyme, l-aspartate semialdehyde, l-aspartate semialdehyde dehydrogenase, phosphate, oxidoreductase
Biological sourceHaemophilus influenzae Rd
Total number of polymer chains1
Total formula weight40781.76
Authors
Blanco, J.,Moore, R.A.,Faehnle, C.R.,Viola, R.E. (deposition date: 2003-06-18, release date: 2004-08-10, Last modification date: 2011-07-13)
Primary citationBlanco, J.,Coe, D.M.,Faehnle, C.R.,Moore, R.A.,Viola, R.E.
The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
Acta Crystallogr.,Sect.D, 60:1388-1395, 2004
PubMed: 15272161
DOI: 110.1107/S0907444904012971
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.06 Å)
Structure validation
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PDB entries from 2021-06-16