Structure of PDB 1vm6 Chain C

Receptor sequence
>1vm6C (length=215) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKYGIVGYSGRMGQEIQKVFSEKGHELVLKVDVNGVEELDSPDVVIDFSS
PEALPKTVDLCKKYRAGLVLGTTALKEEHLQMLRELSKEVPVVQAYNFSI
GINVLKRFLSELVKVLEDWDVEIVETHHRFKKDAPSGTAILLESALGKSV
PIHSLRVGGVPGDHVVVFGNIGETIEIKHRAISRTVFAIGALKAAEFLVG
KDPGMYSFEEVIFGG
3D structure
PDB1vm6 Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution
ChainC
Resolution2.27 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H127 K131
Catalytic site (residue number reindexed from 1) H127 K131
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 C G7 S9 G10 R11 M12 D32 V33 F48 S49 S50 E52 A53 G71 T72 T73 Y96 N97 F98 F187 G7 S9 G10 R11 M12 D32 V33 F48 S49 S50 E52 A53 G71 T72 T73 Y96 N97 F98 F187
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:1vm6, PDBe:1vm6, PDBj:1vm6
PDBsum1vm6
PubMed
UniProtQ9X1K8|DAPB_THEMA 4-hydroxy-tetrahydrodipicolinate reductase (Gene Name=dapB)

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