Structure of PDB 3eia Chain A

Receptor sequence
>3eiaA (length=412) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
EYKTKVSRNSNMSKLQAGYLFPEIARRRSAHLLKYPDAQVISLGIGDTTE
PIPEVITSAMAKKAHELSTIEGYSGYGAEQGAKPLRAAIAKTFYGGLGIG
DDDVFVSDGAKCDISRLQVMFGSNVTIAVQDPSYPAYVDSSVIMGQTGQF
NTDVQKYGNIEYMRCTPENGFFPDLSTVGRTDIIFFCSPNNPTGAAATRE
QLTQLVEFAKKNGSIIVYDSAYAMYMSDDNPRSIFEIPGAEEVAMETASF
SQYAGFTGVRLGWTVIPKKLLYSDGFPVAKDFNRIICTCFNGASNISQAG
ALACLTPEGLEAMHKVIGFYKENTNIIIDTFTSLGYDVYGGKNAPYVWVH
FPNQSSWDVFAEILEKTHVVTTPGSGFGPGGEGFVRVSAFGHRENILEAC
RRFKQLYKHHHH
3D structure
PDB3eia Mechanism of substrate recognition and PLP-induced conformational changes in LL-diaminopimelate aminotransferase from Arabidopsis thaliana.
ChainA
Resolution1.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.83: LL-diaminopimelate aminotransferase.
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 PL6 A Y37 F39 I63 G64 G127 A128 K129 Y152 N209 D237 Y240 S267 S269 R278 R404 Y19 F21 I45 G46 G109 A110 K111 Y134 N191 D219 Y222 S249 S251 R260 R386
BS02 PL6 A Y94 N309 Y76 N291
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0008483 transaminase activity
GO:0010285 L,L-diaminopimelate aminotransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009507 chloroplast
GO:0009570 chloroplast stroma

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3eia, PDBe:3eia, PDBj:3eia
PDBsum3eia
PubMed18952095
UniProtQ93ZN9|DAPAT_ARATH LL-diaminopimelate aminotransferase, chloroplastic (Gene Name=DAP)

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