Structure of PDB 2cdq Chain B

Receptor sequence
>2cdqB (length=470) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
KGITCVMKFGGSSVASAERMKEVADLILTFPEESPVIVLSAMGKTTNNLL
LAGEKAVSCGVSNASEIEELSIIKELHIRTVKELNIDPSVILTYLEELEQ
LLKGIAMMKELTLRTRDYLVSFGECLSTRIFAAYLNTIGVKARQYDAFEI
GFITTDDFTNGDILEATYPAVAKRLYDDWMHDPAVPIVTGFLGKGWKTGA
VTTLGRGGSDLTATTIGKALGLKEIQVWKDVDGVLTCDPTIYKRATPVPY
LTFDEAAELAYFGAQVLHPQSMRPAREGEIPVRVKNSYNPKAPGTIITKT
RDMTKSILTSIVLKRNVTMLDIASTRMLGQVGFLAKVFSIFEELGISVDV
VATSEVSISLTLDPSKLWSRELIQQELDHVVEELEKIAVVNLLKGRAIIS
LIGNVQHSSLILERAFHVLYTKGVNVQMISQGASKVNISFIVNEAEAEGC
VQALHKSFFESGDLSELLIQ
3D structure
PDB2cdq A Novel Organization of Act Domains in Allosteric Enzymes Revealed by the Crystal Structure of Arabidopsis Aspartate Kinase
ChainB
Resolution2.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.2.4: aspartate kinase.
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 B M351 Q354 V355 F357 M327 Q330 V331 F333
BS02 LYS B S371 V372 D373 S347 V348 D349
BS03 LYS B S64 T70 E148 F215 S233 S40 T46 E124 F191 S209
BS04 SAM B G369 I370 S371 D387 W392 S393 R394 L396 E400 G345 I346 S347 D363 W368 S369 R370 L372 E376
Gene Ontology
Molecular Function
GO:0004072 aspartate kinase activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate

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Molecular Function
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Biological Process
External links
PDB RCSB:2cdq, PDBe:2cdq, PDBj:2cdq
PDBsum2cdq
PubMed16731588
UniProtQ9LYU8|AK1_ARATH Aspartokinase 1, chloroplastic (Gene Name=AK1)

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