Structure of PDB 2hs4 Chain A

Receptor sequence
>2hs4A (length=602) Species: 2336 (Thermotoga maritima) [Search protein sequence]
KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRLPKTGFE
GNAGVVNLDDYYSVAFKIESHNHPSAIEPYNGAATGVGGIIRDVLAMGAR
PTAIFDSLHMSRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVN
VLAAGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGASFASEDLTGDK
ATKLSIQVGDPFAEKMLIEAFLEMVEEGLVEGAQDLGAGGVLSATSELVA
KGNLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPQKASRILEIA
RKHLLFGDVVAEVIEEPVYRVMYRNDLVMEVPVQLLANAPEEDIVEYTPG
KIPEFKRVEFEEVNAREVFEQYDHMVGTDTVVPPGFGAAVMRIKRDGGYS
LVTHSRADLALQDTYWGTLIAVLESVRKTLSVGAEPLAITNCVNYGDPDV
DPVGLSAMMTALKNACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLGK
VNPQKVAKPKPSKVFAVGWNDFELEREKELWRAIRKLSEEGAFILSSSQL
LTRTHVETFREYGLKIEVKLPEVRPAHQMVLVFSERTPVVDVPVKEIGTL
SR
3D structure
PDB2hs4 Complexed Structures of Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima Describe a Novel ATP Binding Protein Superfamily
ChainA
Resolution2.7 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 D93 D235
BS02 ACP A Y35 I42 N53 E70 N442 S476 G477 N478 Y34 I41 N52 E69 N441 S475 G476 N477
BS03 FGR A H32 S71 H72 N73 H74 P75 R93 G189 A193 Q208 A239 E280 Q282 S480 H31 S70 H71 N72 H73 P74 R92 G188 A192 Q207 A238 E279 Q281 S479
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:2hs4, PDBe:2hs4, PDBj:2hs4
PDBsum2hs4
PubMed17154526
UniProtQ9X0X3|PURL_THEMA Phosphoribosylformylglycinamidine synthase subunit PurL (Gene Name=purL)

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