Structure of PDB 1yxd Chain A

Receptor sequence
>1yxdA (length=292) Species: 562 (Escherichia coli) [Search protein sequence]
MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESAT
LNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGC
LTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGR
LAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGH
GVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPI
PVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
3D structure
PDB1yxd The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T44 Y107 Y133 R138 K161 I203
Catalytic site (residue number reindexed from 1) T44 Y107 Y133 R138 K161 I203
Enzyme Commision number 4.3.3.7: 4-hydroxy-tetrahydrodipicolinate synthase.
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 LYS A A49 L51 H53 H56 Y106 A49 L51 H53 H56 Y106 PDBbind-CN: -logKd/Ki=5.30,Ki=5uM
BS02 LYS A N80 E84 N80 E84 PDBbind-CN: -logKd/Ki=5.30,Ki=5uM
Gene Ontology
Molecular Function
GO:0008840 4-hydroxy-tetrahydrodipicolinate synthase activity
GO:0016829 lyase activity
GO:0042802 identical protein binding
Biological Process
GO:0009085 lysine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0019877 diaminopimelate biosynthetic process
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1yxd, PDBe:1yxd, PDBj:1yxd
PDBsum1yxd
PubMed16041077
UniProtP0A6L2|DAPA_ECOLI 4-hydroxy-tetrahydrodipicolinate synthase (Gene Name=dapA)

[Back to BioLiP]