Structure of PDB 4tts Chain A Binding Site BS01

Receptor Information
>4tts Chain A (length=308) Species: 7955 (Danio rerio) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKIAVIGQSLFGQEVYKELKNEGHMIVGVFTIPDKDGKVDPLAIEAEKDG
VPVFKFPRWRLKGKAITEVVDQYKAVGAELNVLPFCSQFIPMEVIDHPKH
GSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTVFWADDGLDTGPILLQR
ECDVEPNDNVNSIYKRFLFPEGVKGMVEAVRLIATGKAPRIKQPEEGATA
ECIQKKENSKIDWNQPAEAIHNWIRGNDRVPGAWAEIDGKSVSFYGSTLL
ENDHFSSNGQPLEIPGASRAALVTKNGLVLFGNDGKMLLVKNLQFEDGKM
IPGSQYFK
Ligand information
Ligand ID6DD
InChIInChI=1S/C22H21N5O7/c23-22-25-16-6-1-12(9-15(16)20(32)26-22)10-27(11-28)14-4-2-13(3-5-14)19(31)24-17(21(33)34)7-8-18(29)30/h1-6,9,11,17H,7-8,10H2,(H,24,31)(H,29,30)(H,33,34)(H3,23,25,26,32)/t17-/m0/s1
InChIKeyQHUBQNFYSLRYQG-KRWDZBQOSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Nc1nc(O)c2cc(CN(C=O)c3ccc(cc3)C(=O)N[C@@H](CCC(O)=O)C(O)=O)ccc2n1
CACTVS 3.385Nc1nc(O)c2cc(CN(C=O)c3ccc(cc3)C(=O)N[CH](CCC(O)=O)C(O)=O)ccc2n1
OpenEye OEToolkits 1.9.2c1cc(ccc1C(=O)NC(CCC(=O)O)C(=O)O)N(Cc2ccc3c(c2)c(nc(n3)N)O)C=O
OpenEye OEToolkits 1.9.2c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)N(Cc2ccc3c(c2)c(nc(n3)N)O)C=O
ACDLabs 12.01O=C(O)C(NC(=O)c1ccc(cc1)N(C=O)Cc3cc2c(nc(nc2O)N)cc3)CCC(=O)O
FormulaC22 H21 N5 O7
NameN-(4-{[(2-amino-4-hydroxyquinazolin-6-yl)methyl](formyl)amino}benzoyl)-L-glutamic acid
ChEMBLCHEMBL532231
DrugBank
ZINC
PDB chain4tts Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4tts Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		R58 S87 Q88 F89 I90 I104 G115 A116 D138 G140 L141 D142
Binding residue
(residue number reindexed from 1)		R58 S87 Q88 F89 I90 I104 G115 A116 D138 G140 L141 D142
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) H106 D142
Catalytic site (residue number reindexed from 1) H106 D142
Enzyme Commision number 1.5.1.6: formyltetrahydrofolate dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
Biological Process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4tts, PDBe:4tts, PDBj:4tts
PDBsum4tts
PubMed25849409
UniProtE3NZ06

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