Structure of PDB 5z2f Chain A

Receptor sequence
>5z2fA (length=265) Species: 1231057 (Paenisporosarcina sp. TG-14) [Search protein sequence]
MMIRVAIGGPRGKMGQEAVHTVMNNENMELVAVLDHKDIGDLLSESPNFP
ASYEVPVFLNLESLIVTIKPDVFLDLTTPHQVFEHTMLCLQNNVRPVIGT
TGFTDEQLQQCTILAEVNKLGCIVAPNFAIGAVLMMKFASLAAAYFPDVE
IIEMHHDQKLDAPSGTAYKTAQMIAEVRPSHKQGHPNEKETLEGARGASY
DGIPIHSVRLPGLIAHQQILFGGEGQLFTLRHDSYNRQSFMSGVTFSINQ
VMEIKELVYGLENIL
3D structure
PDB5z2f Crystal structure of dihydrodipicolinate reductase (PaDHDPR) from Paenisporosarcina sp. TG-14: structural basis for NADPH preference as a cofactor
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
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 NAP A R10 G11 K12 M13 D34 H35 K36 L75 T76 G98 T99 T100 P125 N126 F127 R11 G12 K13 M14 D35 H36 K37 L76 T77 G99 T100 T101 P126 N127 F128
BS02 PDC A P125 H154 H155 K158 S163 G164 T165 A214 P126 H155 H156 K159 S164 G165 T166 A215
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5z2f, PDBe:5z2f, PDBj:5z2f
PDBsum5z2f
PubMed29786696
UniProtA0A3B6UER2

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