Structure of PDB 3ijp Chain B

Receptor sequence

>3ijpB (length=267) Species: 38323 (Bartonella henselae)

SMRLTVVGANGRMGRELITAIQRRKDVELCAVLVRKGSSFVDKDASILIG
SDFLGVRITDDPESAFSNTEGILDFSQPQASVLYANYAAQKSLIHIIGTT
GFSKTEEAQIADFAKYTTIVKSGNMSLGVNLLANLVKRAAKALDDDFDIE
IYEMHHANKVDSPSGTALLLGQAAAEGRNIMLKNVSVNGRSGHTGKREKG
TIGFACSRGGTVIGDHSITFAGENERIVLSHIAQERSIFANGALKAALWA
KNHENGLYSMLDVLGLN

3D structure

• PDB: 3ijp The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 angstrom resolution.
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H154 K158
• Catalytic site (residue number reindexed from 1): H155 K159
• 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	NA	B	I20 Q21 R23 V26 E27	I21 Q22 R24 V27 E28

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:0050661 NADP binding
• GO:0051287 NAD binding

Biological Process

• GO:0009085 lysine biosynthetic process
• GO:0009089 lysine biosynthetic process via diaminopimelate
• GO:0019877 diaminopimelate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3ijp, PDBe:3ijp, PDBj:3ijp
• PDBsum: 3ijp
• PubMed: 27917836
• UniProt: Q6G2G3|DAPB_BARHE 4-hydroxy-tetrahydrodipicolinate reductase (Gene Name=dapB)