Structure of PDB 1frw Chain A Binding Site BS02

Receptor Information
>1frw Chain A (length=185) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLMTTITGVVLAGGKVDKGLLELNGKPLWQHVADALMTQLSHVVVNANRH
QEIYQASGLKVIEDSLADYPGPLAGMLSVMQQEAGEWFLFCPCDTPYIPP
DLAARLNHQRKDAPVVWVHDGERDHPTIALVNRAIEPLLLEYLQAGERRV
MVFMRLAGGHAVDFSDHKDAFVNVNTPEELARWQE
Ligand information
Ligand IDGTP
InChIInChI=1S/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKeyXKMLYUALXHKNFT-UUOKFMHZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
FormulaC10 H16 N5 O14 P3
NameGUANOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL1233147
DrugBankDB04137
ZINCZINC000060094177
PDB chain1frw Chain A Residue 198 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1frw The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis.
Resolution1.75 Å
Binding residue
(original residue number in PDB)		L12 A13 G14 G15 K25 N53 D71 G78 P79 G82 P99 D101
Binding residue
(residue number reindexed from 1)		L11 A12 G13 G14 K18 N46 D64 G71 P72 G75 P92 D94
Annotation score4
Enzymatic activity
Enzyme Commision number 2.7.7.77: molybdenum cofactor guanylyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016740 transferase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0061603 molybdenum cofactor guanylyltransferase activity
GO:0070568 guanylyltransferase activity
Biological Process
GO:0006777 Mo-molybdopterin cofactor biosynthetic process
GO:0019720 Mo-molybdopterin cofactor metabolic process
GO:1902758 bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1frw, PDBe:1frw, PDBj:1frw
PDBsum1frw
PubMed10978347
UniProtP32173|MOBA_ECOLI Molybdenum cofactor guanylyltransferase (Gene Name=mobA)

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