Structure of PDB 1arz Chain C

Receptor sequence

>1arzC (length=271) Species: 83333 (Escherichia coli K-12)

DANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGEL
AGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIG
TTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTD
IEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERV
PGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSAL
WLSGKESGLFDMRDVLDLNNL

3D structure

• PDB: 1arz Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate.
• Chain: C
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H159 K163
• Catalytic site (residue number reindexed from 1): H157 K161
• 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	NAI	C	G12 G15 R16 M17 E38 F79 T80 R81 G84 G102 T104 A127 F129 F243	G10 G13 R14 M15 E36 F77 T78 R79 G82 G100 T102 A125 F127 F241
BS02	PDC	C	T104 K163 S168 G169 T170	T102 K161 S166 G167 T168

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)