Structure of PDB 2hs0 Chain A

Receptor sequence
>2hs0A (length=580) Species: 2336 (Thermotoga maritima) [Search protein sequence]
KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGFE
GNAGVVNLDDYYSVAFKIESHNHPSAIEPYNGAATGVGGIIRDVLAMGAR
PTAIFDSLHMSRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVN
VLAAGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIIQVGDPFAEKMLIE
AFLEMVEEGLVEGAQDLGAGGVLSATSELVAKGNLGAIVHLDRVPLREPD
MEPWEILISESQERMAVVTSPQKASRILEIARKHLLFGDVVAEVIEEPVY
RVMYRNDLVMEVPVQLLANAPEEDIVEYTPGKIPEFKRVEFEEVNAREVF
EQYDGTDTVVPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTLIAV
LESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMMTALKNACEFSGVP
VASGNASLYNTYQGKPIPPTLVVGMLGKVNPQKVAKPKPSKVFAVGWNDF
ELEREKELWRAIRKLSEEGAFILSSSQLLTRTHVETFREYGLKIEVKLPE
VRPAHQMVLVFSERTPVVDVPVKEIGTLSR
3D structure
PDB2hs0 Complexed Structures of Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima Describe a Novel ATP Binding Protein Superfamily
ChainA
Resolution2.52 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.5.3: phosphoribosylformylglycinamidine synthase.
Interaction with ligand
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2hs0, PDBe:2hs0, PDBj:2hs0
PDBsum2hs0
PubMed17154526
UniProtQ9X0X3|PURL_THEMA Phosphoribosylformylglycinamidine synthase subunit PurL (Gene Name=purL)

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