Structure of PDB 1fhi Chain A Binding Site BS01

Receptor Information
>1fhi Chain A (length=125) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLR
PDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLP
RKAGDSWRSEEEMAAEAAALRVYFQ
Ligand information
Ligand IDIB2
InChIInChI=1S/C21H29N10O14P3S/c22-16-10-18(26-3-24-16)30(5-28-10)20-14(34)12(32)8(43-20)1-41-46(36,37)7-47(38,39)45-48(40,49)42-2-9-13(33)15(35)21(44-9)31-6-29-11-17(23)25-4-27-19(11)31/h3-6,8-9,12-15,20-21,32-35H,1-2,7H2,(H,36,37)(H,38,39)(H,40,49)(H2,22,24,26)(H2,23,25,27)/t8-,9-,12-,13-,14-,15-,20-,21-,48-/m1/s1
InChIKeyUJCWOSLCGXVJOD-LCHUORCTSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(C[P@](=O)(O)O[P@@](=O)(OC[C@@H]4[C@H]([C@H]([C@@H](O4)n5cnc6c5ncnc6N)O)O)S)O)O)O)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(CP(=O)(O)OP(=O)(OCC4C(C(C(O4)n5cnc6c5ncnc6N)O)O)S)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)C[P@@](O)(=O)O[P@@](S)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)n5cnc6c(N)ncnc56)[C@@H](O)[C@H]3O
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)C[P](O)(=O)O[P](S)(=O)OC[CH]4O[CH]([CH](O)[CH]4O)n5cnc6c(N)ncnc56)[CH](O)[CH]3O
FormulaC21 H29 N10 O14 P3 S
NameP1-P2-METHYLENE-P3-THIO-DIADENOSINE TRIPHOSPHATE;
ADO-P-CH2-P-PS-ADO
ChEMBL
DrugBankDB04389
ZINC
PDB chain1fhi Chain A Residue 301 [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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PDB1fhi Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		F5 I10 N27 T79 S81 Q83 T91 V92 H96 H98 L100 R102
Binding residue
(residue number reindexed from 1)		F4 I9 N26 T78 S80 Q82 T90 V91 H95 H97 L99 R101
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) Q83 H94 H96 H98
Catalytic site (residue number reindexed from 1) Q82 H93 H95 H97
Enzyme Commision number 2.7.7.51: adenylylsulfate--ammonia adenylyltransferase.
3.6.1.29: bis(5'-adenosyl)-triphosphatase.
3.6.2.1: adenylylsulfatase.
3.9.1.-
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0031625 ubiquitin protein ligase binding
GO:0042802 identical protein binding
GO:0043530 adenosine 5'-monophosphoramidase activity
GO:0047352 adenylylsulfate-ammonia adenylyltransferase activity
GO:0047627 adenylylsulfatase activity
GO:0047710 bis(5'-adenosyl)-triphosphatase activity
Biological Process
GO:0006163 purine nucleotide metabolic process
GO:0006915 apoptotic process
GO:0015964 diadenosine triphosphate catabolic process
GO:0032435 negative regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0072332 intrinsic apoptotic signaling pathway by p53 class mediator
Cellular Component
GO:0001650 fibrillar center
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fhi, PDBe:1fhi, PDBj:1fhi
PDBsum1fhi
PubMed9576908
UniProtP49789|FHIT_HUMAN Bis(5'-adenosyl)-triphosphatase (Gene Name=FHIT)

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