Structure of PDB 1pqu Chain D

Receptor sequence
>1pquD (length=371) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence]
MKNVGFIGWRGMVGSVLMDRMSQENDFENLNPVFFTTSQAGQKAPVFGGK
DAGDLKSAFDIEELKKLDIIVTCQGGDYTNEVYPKLKATGWDGYWVDAAS
ALRMKDDAIIVLDPVNQHVISEGLKKGIKTFVGGNCTVSLMLMAIGGLFE
KDLVEWISVATYQAASGAGAKNMRELLSQMGLLEQAVSSELKDPASSILD
IERKVTAKMRADNFPTDNFGAALGGSLIPWIDKLLPETGQTKEEWKGYAE
TNKILGLSDNPIPVDGLCVRIGALRCNSQAFTIKLKKDLPLEEIEQIIAS
HNEWVKVIPNDKEITLRELTPAKVTGTLSVPVGRLRKLAMGPEYLAAFTV
GDQLLWGAAEPVRRILKQLVA
3D structure
PDB1pqu The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
ChainD
Resolution1.92 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C136 Q163 R270 N277
Catalytic site (residue number reindexed from 1) C136 Q163 R270 N277
Enzyme Commision number 1.2.1.11: aspartate-semialdehyde dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAP D G8 R10 G11 M12 V13 T36 T37 C73 Q74 G75 A99 S166 G167 Q353 L354 A358 G8 R10 G11 M12 V13 T36 T37 C73 Q74 G75 A99 S166 G167 Q353 L354 A358
BS02 CYS D C136 Q163 G167 E243 R270 Q353 C136 Q163 G167 E243 R270 Q353
Gene Ontology
Molecular Function
GO:0004073 aspartate-semialdehyde dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046983 protein dimerization activity
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0009088 threonine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0009097 isoleucine biosynthetic process
GO:0019877 diaminopimelate biosynthetic process
GO:0071266 'de novo' L-methionine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1pqu, PDBe:1pqu, PDBj:1pqu
PDBsum1pqu
PubMed15272161
UniProtP44801|DHAS_HAEIN Aspartate-semialdehyde dehydrogenase (Gene Name=asd)

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