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Structure of PDB 4nog Chain B Binding Site BS01

Receptor Information >4nog Chain B (length=424) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] ARKTNIEAYRDGLKLKTEEDFFACDRQYVCQNYAPVPVVISKGKGARVWD INGNEYYDFLAGVSSLSQGHCHPRVIAALCRQAERLTLTLRAFGNDVTGP ACRFMAEMFGYDRVLLMNTGAEAGESALKIARKWAYEVKEIPPDSAKVIL CNNNYWGRTITACSSSTTFDCYNNFGPFTPGFELIDYDDVGALEEALKDP NVAAFFVEPIQGEGGVNVPKPGYLKRAHELCRSKNVLLIVDEIQTGLCRT GRLLAADHDEVHPDILLLGKSLSAGVVPISAVMGRADVMDVLKPGTHGST FGGNPLACAVAVEALTVLKDEKLADRAERLGAQFRDCLRRELYGKVPWIK EIRGRGLLNAVEVDSDAIDPNDVVMKLKENGILSKPTRGRVMRFIPPLVI TDEEHRDATTRIIKSFLAVEEERK

Ligand information Ligand ID PLP InChI InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14) InChIKey NGVDGCNFYWLIFO-UHFFFAOYSA-N SMILES Software SMILES CACTVS 3.341 Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O OpenEye OEToolkits 1.5.0 Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O ACDLabs 10.04 O=P(O)(O)OCc1cnc(c(O)c1C=O)C Formula C8 H10 N O6 P Name PYRIDOXAL-5'-PHOSPHATE; VITAMIN B6 Phosphate ChEMBL CHEMBL82202 DrugBank DB00114 ZINC ZINC000001532514 PDB chain 4nog Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 4nog CSGID Solves Structures and Identifies Phenotypes for Five Enzymes in Toxoplasma gondii . Resolution 1.2 Å Binding residue (original residue number in PDB) G136 A137 Y171 W172 D257 I259 Q260 K286 Binding residue (residue number reindexed from 1) G120 A121 Y155 W156 D241 I243 Q244 K270 Annotation score 1

Enzymatic activity Catalytic site (original residue number in PDB) Y171 E224 D257 Q260 K286 T316 R409 Catalytic site (residue number reindexed from 1) Y155 E208 D241 Q244 K270 T300 R393 Enzyme Commision number 2.6.1.13: ornithine aminotransferase.

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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