Structure of PDB 5dj9 Chain A

Receptor sequence
>5dj9A (length=421) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence]
KTNIEAYRDGLKLKTEEDFFACDRQYVCQNYAPVPVVISKGKGARVWDIN
GNEYYDFLAGVSSLSQGHCHPRVIAALCRQAERLTLTLRAFGNDVTGPAC
RFMAEMFGYDRVLLMNTGAEAGESALKIARKWAYEVKEIPPDSAKVILCN
NNYWGRTITACSSSTTFDCYNNFGPFTPGFELIDYDDVGALEEALKDPNV
AAFFVEPIQGEGGVNVPKPGYLKRAHELCRSKNVLLIVDEIQTGLCRTGR
LLAADHDEVHPDILLLGKSLSAGVVPISAVMGRADVMDVLKPGTHGSTFG
GNPLACAVAVEALTVLKDEKLADRAERLGAQFRDCLRRELYGKVPWIKEI
RGRGLLNAVEVDSDAIDPNDVVMKLKENGILSKPTRGRVMRFIPPLVITD
EEHRDATTRIIKSFLAVEEER
3D structure
PDB5dj9 Crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49 in a complex with gabaculine
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y171 E224 D257 Q260 K286 T316 R409
Catalytic site (residue number reindexed from 1) Y153 E206 D239 Q242 K268 T298 R391
Enzyme Commision number 2.6.1.13: ornithine 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 PXG A Y49 V79 G136 A137 Y171 W172 E229 D257 I259 Q260 K286 Y31 V61 G118 A119 Y153 W154 E211 D239 I241 Q242 K268
BS02 PXG A S315 T316 S297 T298
Gene Ontology
Molecular Function
GO:0004587 ornithine aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0010121 arginine catabolic process to proline via ornithine
GO:0019544 arginine catabolic process to glutamate
GO:0055129 L-proline biosynthetic process
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:5dj9, PDBe:5dj9, PDBj:5dj9
PDBsum5dj9
PubMed
UniProtS8EY38

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