BioLiP

Receptor Information

>1njs Chain B (length=200) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAG
IPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKW
NGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIIL
QEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWV

Ligand ID

KEU

InChI

InChI=1S/C22H30F3N5O8/c23-22(24,25)21(37,38)13(3-1-2-12-16(26)29-20(27)30-18(12)34)10-4-6-11(7-5-10)17(33)28-14(19(35)36)8-9-15(31)32/h4-7,12-14,16,20,29,37-38H,1-3,8-9,26-27H2,(H,28,33)(H,30,34)(H,31,32)(H,35,36)/t12?,13-,14+,16+,20-/m1/s1

InChIKey

KOLDLUFBEMUZIM-YNPGLMGXSA-N

SMILES

Software	SMILES
CACTVS 3.341	N[CH]1N[CH](N)[CH](CCC[CH](c2ccc(cc2)C(=O)N[CH](CCC(O)=O)C(O)=O)C(O)(O)C(F)(F)F)C(=O)N1
ACDLabs 10.04	O=C1NC(N)NC(N)C1CCCC(c2ccc(C(=O)NC(C(=O)O)CCC(=O)O)cc2)C(O)(O)C(F)(F)F
OpenEye OEToolkits 1.5.0	c1cc(ccc1C(CCCC2C(NC(NC2=O)N)N)C(C(F)(F)F)(O)O)C(=O)NC(CCC(=O)O)C(=O)O
OpenEye OEToolkits 1.5.0	c1cc(ccc1[C@@H](CCCC2C(NC(NC2=O)N)N)C(C(F)(F)F)(O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)O
CACTVS 3.341	N[C@@H]1N[C@H](N)[C@H](CCC[C@H](c2ccc(cc2)C(=O)N[C@@H](CCC(O)=O)C(O)=O)C(O)(O)C(F)(F)F)C(=O)N1

Formula

C22 H30 F3 N5 O8

Name

N-{4-[(1R)-4-[(2R,4R,5S)-2,4-DIAMINO-6-OXOHEXAHYDROPYRIMIDIN-5-YL]-1-(2,2,2-TRIFLUORO-1,1-DIHYDROXYETHYL)BUTYL]BENZOYL}-D-GLUTAMIC ACID;
10-CF3C(OH)2-DDACTHF;
HYDROLYZED FORM OF 10-TRIFLUOROACETYL-5,10-DIDEAZA-ACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID

PDB chain

1njs Chain B Residue 610 [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]

PDB	1njs Rational Design, Synthesis, Evaluation, and Crystal Structure of a Potent Inhibitor of Human GAR Tfase: 10-(Trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic Acid
Resolution	1.98 Å
Binding residue (original residue number in PDB)	R64 L85 M89 R90 I91 L92 N106 H108 G117 V139 A140 V143 D144
Binding residue (residue number reindexed from 1)	R64 L85 M89 R90 I91 L92 N106 H108 G117 V139 A140 V143 D144
Annotation score	1
Binding affinity	MOAD: Ki=15nM

Catalytic site (original residue number in PDB)	N106 H108 T135 D144
Catalytic site (residue number reindexed from 1)	N106 H108 T135 D144
Enzyme Commision number	2.1.2.2: phosphoribosylglycinamide formyltransferase 1. 6.3.3.1: phosphoribosylformylglycinamidine cyclo-ligase. 6.3.4.13: phosphoribosylamine--glycine ligase.

	Molecular Function
GO:0004644	phosphoribosylglycinamide formyltransferase activity

	Biological Process
GO:0006189	'de novo' IMP biosynthetic process
GO:0009058	biosynthetic process

PDB	RCSB:1njs, PDBe:1njs, PDBj:1njs
PDBsum	1njs
PubMed	12755606
UniProt	P22102\|PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 (Gene Name=GART)

[Back to BioLiP]

Structure of PDB 1njs Chain B Binding Site BS01