Structure of PDB 6jrq Chain A

Receptor sequence
>6jrqA (length=407) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
PGIAIIGAQWGDEGKGKVVDVLAREADYVIRYQGGANAGHTVVAEGKVFK
LNLLPSGVIHPHAVNVLGDGMVIDPFRFQEEVEGLRKEGFDPKILVSERA
HLVLPHHKHVESRHNFVGTTGRGIGPAYSDRARRVGIRAGDLLDEATLRE
RVRRLLAEKPNSTREAGWDTEEKALADLHRMREILSPYIADTGSLLREAW
RKGKRLLFEGAQATLLDLNYGTYPYVTSSHPTVGGILVGTGLSHKAITKV
YGVAKAYTTRVGEGPFPTELQGELAHHLREKGGEYGTTTGRPRRVGWLDL
VALRYACEVNGFDGLVLTKLDVLSGLEKVKVAVEYLDGARPGEASPEAVR
YLELPGWGDLSHVKRREDLPANLLRYLELVEEHTGVPVVLFSTSPRREDT
FGAVSWV
3D structure
PDB6jrq Crystal structure of adenylosuccinate synthetase, PurA, from Thermus thermophilus HB8
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D13 K16 G40 H41 Q213
Catalytic site (residue number reindexed from 1) D12 K15 G39 H40 Q212
Enzyme Commision number 6.3.4.4: adenylosuccinate 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 IMP A D13 N38 T120 T121 Q213 L217 V227 T228 V262 D12 N37 T119 T120 Q212 L216 V226 T227 V261
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004019 adenylosuccinate synthase activity
GO:0005525 GTP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
GO:0046040 IMP metabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:6jrq, PDBe:6jrq, PDBj:6jrq
PDBsum6jrq
PubMed
UniProtQ5SLS1|PURA_THET8 Adenylosuccinate synthetase (Gene Name=purA)

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