Structure of PDB 1drw Chain A

Receptor sequence

>1drwA (length=272) Species: 562 (Escherichia coli)

HDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGE
LAGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVI
GTTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYT
DIEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGER
VPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSA
LWLSGKESGLFDMRDVLDLNNL

3D structure

• PDB: 1drw Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H159 K163
• Catalytic site (residue number reindexed from 1): H158 K162
• Enzyme Commision number: 1.17.1.8: 4-hydroxy-tetrahydrodipicolinate reductase.

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	NHD	A	G12 G15 R16 M17 E38 R39 F79 T80 R81 G102 T103 T104 A127 N128 F129 F243	G11 G14 R15 M16 E37 R38 F78 T79 R80 G101 T102 T103 A126 N127 F128 F242	MOAD: Kd=1.48uM

Gene Ontology

Molecular Function

• GO:0008839 4-hydroxy-tetrahydrodipicolinate reductase
• GO:0016491 oxidoreductase activity
• GO:0016726 oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
• GO:0042802 identical protein binding
• GO:0050661 NADP binding
• GO:0051287 NAD binding

Biological Process

• GO:0008652 amino acid biosynthetic process
• GO:0009085 lysine biosynthetic process
• GO:0009089 lysine biosynthetic process via diaminopimelate
• GO:0019877 diaminopimelate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1drw, PDBe:1drw, PDBj:1drw
• PDBsum: 1drw
• PubMed: 8873595
• UniProt: P04036|DAPB_ECOLI 4-hydroxy-tetrahydrodipicolinate reductase (Gene Name=dapB)