Structure of PDB 7ted Chain G Binding Site BS01

Receptor Information
>7ted Chain G (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 G 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)		Y55 Y85 G142 V143 F177 W178 E230 E235 D263 Q266 K292
Binding residue
(residue number reindexed from 1)		Y20 Y50 G107 V108 F142 W143 E195 E200 D228 Q231 K257
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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