Structure of PDB 4nog Chain A

Receptor sequence
>4nogA (length=422) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence]
RKTNIEAYRDGLKLKTEEDFFACDRQYVCQNYAPVPVVISKGKGARVWDI
NGNEYYDFLAGVSSLSQGHCHPRVIAALCRQAERLTLTLRAFGNDVTGPA
CRFMAEMFGYDRVLLMNTGAEAGESALKIARKWAYEVKEIPPDSAKVILC
NNNYWGRTITACSSSTTFDCYNNFGPFTPGFELIDYDDVGALEEALKDPN
VAAFFVEPIQGEGGVNVPKPGYLKRAHELCRSKNVLLIVDEIQTGLCRTG
RLLAADHDEVHPDILLLGKSLSAGVVPISAVMGRADVMDVLKPGTHGSTF
GGNPLACAVAVEALTVLKDEKLADRAERLGAQFRDCLRRELYGKVPWIKE
IRGRGLLNAVEVDSDAIDPNDVVMKLKENGILSKPTRGRVMRFIPPLVIT
DEEHRDATTRIIKSFLAVEEER
3D structure
PDB4nog CSGID Solves Structures and Identifies Phenotypes for Five Enzymes in Toxoplasma gondii .
ChainA
Resolution1.2 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) Y154 E207 D240 Q243 K269 T299 R392
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 PLP A G136 A137 Y171 W172 D257 I259 Q260 K286 G119 A120 Y154 W155 D240 I242 Q243 K269
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:4nog, PDBe:4nog, PDBj:4nog
PDBsum4nog
PubMed30345257
UniProtS8EY38

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