Structure of PDB 2z1z Chain A

Receptor sequence
>2z1zA (length=408) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
EYKTKVSRNSNMSKLQAGYLFPEIARRRSAHLLKYPDAQVISLGIGDTTE
PIPEVITSAMAKKAHELSTIEGYSGYGAEQGAKPLRAAIAKTFYGGLGIG
DDDVFVSDGAKCDISRLQVMFGSNVTIAVQDPSYPAYVDSSVIMGQTGQF
NTDVQKYGNIEYMRCTPENGFFPDLSTVGRTDIIFFCSPNNPTGAAATRE
QLTQLVEFAKKNGSIIVYDSAYAMYMSDDNPRSIFEIPGAEEVAMETASF
SKYAGFTGVRLGWTVIPKKLLYSDGFPVAKDFNRIICTCFNGASNISQAG
ALACLTPEGLEAMHKVIGFYKENTNIIIDTFTSLGYDVYGGKNAPYVWVH
FPNQSSWDVFAEILEKTHVVTTPGSGFGPGGEGFVRVSAFGHRENILEAC
RRFKQLYK
3D structure
PDB2z1z Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia
ChainA
Resolution2.4 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 PLP A G127 A128 K129 Y152 N209 D237 Y240 S267 S269 K270 R278 G109 A110 K111 Y134 N191 D219 Y222 S249 S251 K252 R260
BS02 PLP 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:2z1z, PDBe:2z1z, PDBj:2z1z
PDBsum2z1z
PubMed17583737
UniProtQ93ZN9|DAPAT_ARATH LL-diaminopimelate aminotransferase, chloroplastic (Gene Name=DAP)

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