Structure of PDB 3ijp Chain A

Receptor sequence

>3ijpA (length=266) Species: 38323 (Bartonella henselae)

SMRLTVVGANGRMGRELITAIQRRKDVELCAVLVRKGSSFVDKDASILIG
SDFLGVRITDDPESAFSNTEGILDFSQPQASVLYANYAAQKSLIHIIGTT
GFSKTEEAQIADFAKYTTIVKSGNMSLGVNLLANLVKRAAKALDDDFDIE
IYEMHHANKVDSPSGTALLLGQAAAEGRNIMLKNVSVNGRSGHTGKREKG
TIGFACSRGGTVIGDHSITFAGENERIVLSHIAQERSIFANGALKAALWA
KNHENGLYSMLDVLGL

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: A
• 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	A	I20 Q21 R23 V26	I21 Q22 R24 V27
BS02	NAP	A	G7 N9 G10 R11 M12 R34 F74 S75 Q76 A79 G97 T99 G122 N123 M124 F238	G8 N10 G11 R12 M13 R35 F75 S76 Q77 A80 G98 T100 G123 N124 M125 F239

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)