Structure of PDB 5ten Chain E

Receptor sequence
>5tenE (length=269) Species: 216895 (Vibrio vulnificus CMCP6) [Search protein sequence]
MVRIAVAGAAGRMGRNLVKAAHHNPVAKVAAGSERPESSLVGVDLGELCG
EGKFDVVVCDDLAKQIDQFDVIIDFTAPASTLNNLALCQQYGKSIVIGTT
GFTEEQREQIDLVAQQVPVVMAPNYSVGVNLVFKLLEKAAKVMGDYCDIE
IVEAHHRHKVDAPSGTAIGMGEAIAGAMGNKLSDVAVYAREGITGERTKD
EIGFATIRAGDIVGEHTAMFADIGERVEITHKATDRMTFANGAVKAAVWL
HEKPAGFYTMTDVLGLNDL
3D structure
PDB5ten Comparative structural and mechanistic studies of 4-hydroxy-tetrahydrodipicolinate reductases from Mycobacterium tuberculosis and Vibrio vulnificus.
ChainE
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H155 K159
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 NAD E G8 G11 R12 M13 E34 F75 T76 S80 G98 T100 P123 Y125 F239 G8 G11 R12 M13 E34 F75 T76 S80 G98 T100 P123 Y125 F239
BS02 7FN E T100 H155 H156 K159 G165 T166 T100 H155 H156 K159 G165 T166
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
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:5ten, PDBe:5ten, PDBj:5ten
PDBsum5ten
PubMed32980502
UniProtQ8DEM0|DAPB_VIBVU 4-hydroxy-tetrahydrodipicolinate reductase (Gene Name=dapB)

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