Structure of PDB 7ted Chain I Binding Site BS01

Receptor Information
>7ted Chain I (length=404) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSY
SAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHK
VLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAI
SSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGE
AGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRP
DIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIA
ALEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKET
KDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKT
ILSF
Ligand information
Ligand IDI1T
InChIInChI=1S/C15H21N2O8P/c1-8-14(19)12(11(4-16-8)7-25-26(22,23)24)5-17-13-3-9(15(20)21)2-10(13)6-18/h4,6,9-10,13,17,19H,2-3,5,7H2,1H3,(H,20,21)(H2,22,23,24)/t9-,10-,13-/m0/s1
InChIKeyQPJGRJWUQOEMOU-KWBADKCTSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Cc1[nH+]cc(CO[P](O)(O)=O)c(C[NH2+][CH]2C[CH](C[CH]2C=O)C([O-])=O)c1[O-]
ACDLabs 12.01O=P(O)(O)OCc1c[nH+]c(C)c([O-])c1C[NH2+]C1CC(CC1C=O)C([O-])=O
CACTVS 3.385Cc1[nH+]cc(CO[P](O)(O)=O)c(C[NH2+][C@H]2C[C@H](C[C@H]2C=O)C([O-])=O)c1[O-]
OpenEye OEToolkits 2.0.7Cc1c(c(c(c[nH+]1)COP(=O)(O)O)C[NH2+]C2CC(CC2C=O)C(=O)[O-])[O-]
OpenEye OEToolkits 2.0.7Cc1c(c(c(c[nH+]1)COP(=O)(O)O)C[NH2+][C@H]2C[C@H](C[C@H]2C=O)C(=O)[O-])[O-]
FormulaC15 H21 N2 O8 P
Name(1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid
ChEMBL
DrugBank
ZINC
PDB chain7ted Chain C Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7ted Rational Design, Synthesis, and Mechanism of (3 S ,4 R )-3-Amino-4-(difluoromethyl)cyclopent-1-ene-1-carboxylic Acid: Employing a Second-Deprotonation Strategy for Selectivity of Human Ornithine Aminotransferase over GABA Aminotransferase.
Resolution2.63 Å
Binding residue
(original residue number in PDB)		S321 T322
Binding residue
(residue number reindexed from 1)		S286 T287
Annotation score1
Enzymatic activity
Enzyme Commision number 2.6.1.13: ornithine aminotransferase.
Gene Ontology
Molecular Function
GO:0004587 ornithine aminotransferase activity
GO:0005515 protein binding
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0007601 visual perception
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:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7ted, PDBe:7ted, PDBj:7ted
PDBsum7ted
PubMed35293728
UniProtP04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)

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