Structure of PDB 4pzv Chain A Binding Site BS01

Receptor Information
>4pzv Chain A (length=413) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQYIIGIGTNIGFTIENIHLAITALESQQNIRIIRKASLYSSKAVLKEDA
PKEWDIRFLNTAVKISSSLKPDELLVLLKDIELKIGRDLNAPAWSPRVID
LDILAAEDLILETDKLTIPHKELINRSFALAPLLELSKGWHHPKYVEWDL
NIRLKELGEIVKLKQTLANTIRMGIVNLSSDGNFDDNQRKLNLDELIQSG
AEIIDIGAESTKPISIEEEFNKLDEFLEYFKSQLANLIYKPLVSIDTRKL
EVMQKILAKHHDIIWMINDVECNNIEQKAQLIAKYNKKYVIIHNLGITDR
NQYLDKENAIDNVCDYIEQKKQILLKHGIAQQNIYFDIGFGFGKKSDTAR
YLLENIIEIKRRLELKALVGHSRKPSVLGLAKDSNLATLDRATRELSRKL
EKLDIDIIRVHKI
Ligand information
Ligand IDJ1D
InChIInChI=1S/C23H30N12O8S/c1-23(2)15(31-12-17(34-23)32-22(25)33-19(12)39)20(40)27-5-10(36)26-3-4-44(41,42)6-9-13(37)14(38)21(43-9)35-8-30-11-16(24)28-7-29-18(11)35/h7-9,13-14,21,37-38H,3-6H2,1-2H3,(H,26,36)(H,27,40)(H2,24,28,29)(H4,25,32,33,34,39)/t9-,13-,14-,21-/m1/s1
InChIKeyQCWCABDSXQYDST-GWKRVTOESA-N
SMILES
SoftwareSMILES
CACTVS 3.370CC1(C)NC2=C(N=C1C(=O)NCC(=O)NCC[S](=O)(=O)C[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)C(=O)NC(=N2)N
OpenEye OEToolkits 1.7.6CC1(C(=NC2=C(N1)N=C(NC2=O)N)C(=O)NCC(=O)NCCS(=O)(=O)CC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)C
CACTVS 3.370CC1(C)NC2=C(N=C1C(=O)NCC(=O)NCC[S](=O)(=O)C[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)C(=O)NC(=N2)N
OpenEye OEToolkits 1.7.6CC1(C(=NC2=C(N1)N=C(NC2=O)N)C(=O)NCC(=O)NCCS(=O)(=O)C[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)C
ACDLabs 12.01O=C2NC(=NC=1NC(C(=NC=12)C(=O)NCC(=O)NCCS(=O)(=O)CC5OC(n4cnc3c(ncnc34)N)C(O)C5O)(C)C)N
FormulaC23 H30 N12 O8 S
Name5'-{[2-({N-[(2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)carbonyl]glycyl}amino)ethyl]sulfonyl}-5'-deoxyadenosine
ChEMBLCHEMBL2046607
DrugBank
ZINCZINC000084758446
PDB chain4pzv Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4pzv Structural enzymology and inhibition of the bi-functional folate pathway enzyme HPPK-DHPS from the biowarfare agent Francisella tularensis.
Resolution1.704 Å
Binding residue
(original residue number in PDB)		V45 F58 N60 L75 K79 R87 W94 R97 D100 D102 I103 K115 L116 T117 H120 F128
Binding residue
(residue number reindexed from 1)		V45 F58 N60 L75 K79 R87 W94 R97 D100 D102 I103 K115 L116 T117 H120 F128
Annotation score1
Binding affinityMOAD: Kd=2uM
PDBbind-CN: -logKd/Ki=5.70,Kd=2.0uM
Enzymatic activity
Catalytic site (original residue number in PDB) R87 R97 D100 D102 K382 R417
Catalytic site (residue number reindexed from 1) R87 R97 D100 D102 K374 R409
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0004156 dihydropteroate synthase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0016310 phosphorylation
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4pzv, PDBe:4pzv, PDBj:4pzv
PDBsum4pzv
PubMed24975935
UniProtQ5NGA7

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