Structure of PDB 1arz Chain A

Receptor sequence

>1arzA (length=270) Species: 83333 (Escherichia coli K-12)

ANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELA
GAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGT
TGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDI
EIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERVP
GTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSALW
LSGKESGLFDMRDVLDLNNL

3D structure

• PDB: 1arz Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate.
• Chain: A
• Resolution: 2.6 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	PO4	A	H160 K163	H157 K160

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:1arz, PDBe:1arz, PDBj:1arz
• PDBsum: 1arz
• PubMed: 9398235
• UniProt: P04036|DAPB_ECOLI 4-hydroxy-tetrahydrodipicolinate reductase (Gene Name=dapB)