Structure of PDB 2hry Chain A

Receptor sequence
>2hryA (length=575) Species: 2336 (Thermotoga maritima) [Search protein sequence]
KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGVV
NLDDYYSVAFKIESANHPSAIEPYNGAATGVGGIIRDVLAMGARPTAIFD
SLHMSRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNVLAAGV
VRNDMLVDSKASRPGQVIVIFGGATGRDGIVGDPFAEKMLIEAFLEMVEE
GLVEGAQDLGAGGVLSATSELVAKGNLGAIVHLDRVPLREPDMEPWEILI
SESQERMAVVTSPQKASRILEIARKHLLFGDVVAEVIEEPVYRVMYRNDL
VMEVPVQLLANAPEEDIVEYTPGKIPEFKRVEFEEVNAREVFEQYDHMVG
TDTVVPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTLIAVLESVR
KTLSVGAEPLAITNCVNYGDPDVDPVGLSAMMTALKNACEFSGVPVASGN
ASLYNTYQGKPIPPTLVVGMLGKVNPQKVAKPKPSKVFAVGWNDFELERE
KELWRAIRKLSEEGAFILSSSQLLTRTHVETFREYGLKIEVKLPEVRPAH
QMVLVFSERTPVVDVPVKEIGTLSR
3D structure
PDB2hry Complexed Structures of Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima Describe a Novel ATP Binding Protein Superfamily
ChainA
Resolution2.8 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 MG A D94 D236 D87 D208
BS02 ACP A H32 Y35 I42 K68 E70 D94 G238 A239 N442 S476 G477 N478 H31 Y34 I41 K61 E63 D87 G210 A211 N414 S448 G449 N450
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:2hry, PDBe:2hry, PDBj:2hry
PDBsum2hry
PubMed17154526
UniProtQ9X0X3|PURL_THEMA Phosphoribosylformylglycinamidine synthase subunit PurL (Gene Name=purL)

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