Structure of PDB 1dru Chain A

Receptor sequence

>1druA (length=270) Species: 562 (Escherichia coli)

ANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELA
GAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGT
TGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDI
EIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERVP
GTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSALW
LSGKESGLFDMRDVLDLNNL

3D structure

• PDB: 1dru 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): H156 K160
• 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	NAD	A	G12 G15 R16 M17 E38 R39 F79 T80 R81 G84 G102 T103 T104 A127 N128 F129 F243	G9 G12 R13 M14 E35 R36 F76 T77 R78 G81 G99 T100 T101 A124 N125 F126 F240	MOAD: Kd=0.46uM

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