Structure of PDB 3d54 Chain I

Receptor sequence
>3d54I (length=583) Species: 2336 (Thermotoga maritima) [Search protein sequence]
KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGNA
GVVNLDDYYSVAFKIESHNHPSAIEPYNGAATGVGGIIRDVLAMGARPTA
IFDSLHMSRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNVLA
AGVVRNDMLVDSKASRPGQVIVIFGGATGRDGTKLSIQVGDPFAEKMLIE
AFLEMVEEGLVEGAQDLGAGGVLSATSELVAKGNLGAIVHLDRVPLREPD
MEPWEILISESQERMAVVTSPQKASRILEIARKHLLFGDVVAEVIEEPVY
RVMYRNDLVMEVPVQLLANAPEEDIVEYTPGKIPEFKRVEFEEVNAREVF
EQYDHMVGTDTVVPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTL
IAVLESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMMTALKNACEFS
GVPVASGNASLYNTYQGKPIPPTLVVGMLGKVNPQKVAKPKPSKVFAVGW
NDFELEREKELWRAIRKLSEEGAFILSSSQLLTRTHVETFREYGLKIEVK
LPEVRPAHQMVLVFSERTPVVDVPVKEIGTLSR
3D structure
PDB3d54 Formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima: structural insights into complex formation.
ChainI
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.5.3: phosphoribosylformylglycinamidine synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP I D107 G135 G136 E137 L138 R139 A366 F370 Y373 P385 G386 G388 K429 S548 T553 D103 G131 G132 E133 L134 R135 A346 F350 Y353 P365 G366 G368 K409 S528 T533
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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Cellular Component
External links
PDB RCSB:3d54, PDBe:3d54, PDBj:3d54
PDBsum3d54
PubMed18597481
UniProtQ9X0X3|PURL_THEMA Phosphoribosylformylglycinamidine synthase subunit PurL (Gene Name=purL)

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