Structure of PDB 3ejx Chain D

Receptor sequence
>3ejxD (length=301) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
EKFSPASFLDKKETGVLHFVKYHGLGNDFILVDNRDSSEPKITQEQAAKL
CDRNFGVGADGVIFAMPGVNGTDYAMRIFNSDGSEPEMCGNGVRCFARFI
AELENLQGKHSFTIHTGAGLIVPEIQDDGQVKVDMGTPILKAQDVPTKLS
GNKGEAVVEAELVVDGVSWNVTCVSMGNPHCITFGKKGGPNLKVDDLNLP
EIGPKFEHHEMFPARTNTEFVEVLSRSHLKMRVWERGAGATLACGTGACA
LVVAAVLEGRADRKCTVDLPGGPLEIEWKQEDNHIYMTGPAEAVFYGSAL
L
3D structure
PDB3ejx Crystal structure of diaminopimelate epimerase from Arabidopsis thaliana, an amino acid racemase critical for L-lysine biosynthesis.
ChainD
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C99 H190 E245 C254 G257
Catalytic site (residue number reindexed from 1) C89 H180 E235 C244 G247
Enzyme Commision number 5.1.1.7: diaminopimelate epimerase.
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 ZDP D N37 F39 N90 P96 C99 G100 N101 N188 N227 E245 R246 C254 G255 T256 N27 F29 N80 P86 C89 G90 N91 N178 N217 E235 R236 C244 G245 T246
Gene Ontology
Molecular Function
GO:0008837 diaminopimelate epimerase activity
Biological Process
GO:0009089 lysine biosynthetic process via diaminopimelate
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ejx, PDBe:3ejx, PDBj:3ejx
PDBsum3ejx
PubMed19013471
UniProtQ9LFG2|DAPF_ARATH Diaminopimelate epimerase, chloroplastic (Gene Name=DAPF)

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