Structure of PDB 2hru Chain A Binding Site BS02

Receptor Information
>2hru Chain A (length=581) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGFE
GNAGVVNLDDYYSVAFKIESANHPSAIEPYNGAATGVGGIIRDVLAMGAR
PTAIFDSLHMSRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVN
VLAAGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIVGDPFAEKMLIEAF
LEMVEEGLVEGAQDLGAGGVLSATSELVAKGNLGAIVHLDRVPLREPDME
PWEILISESQERMAVVTSPQKASRILEIARKHLLFGDVVAEVIEEPVYRV
MYRNDLVMEVPVQLLANAPEEDIVEYTPGKIPEFKRVEFEEVNAREVFEQ
YDHMVGTDTVVPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTLIA
VLESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMMTALKNACEFSGV
PVASGNASLYNTYQGKPIPPTLVVGMLGKVNPQKVAKPKPSKVFAVGWND
FELEREKELWRAIRKLSEEGAFILSSSQLLTRTHVETFREYGLKIEVKLP
EVRPAHQMVLVFSERTPVVDVPVKEIGTLSR
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2hru Chain A Residue 902 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2hru Complexed Structures of Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima Describe a Novel ATP Binding Protein Superfamily
Resolution2.8 Å
Binding residue
(original residue number in PDB)		N53 D236
Binding residue
(residue number reindexed from 1)		N52 D214
Annotation score1
Enzymatic activity
Enzyme Commision number 6.3.5.3: phosphoribosylformylglycinamidine synthase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004642 phosphoribosylformylglycinamidine synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2hru, PDBe:2hru, PDBj:2hru
PDBsum2hru
PubMed17154526
UniProtQ9X0X3|PURL_THEMA Phosphoribosylformylglycinamidine synthase subunit PurL (Gene Name=purL)

[Back to BioLiP]