Structure of PDB 6c25 Chain A

Receptor sequence
>6c25A (length=394) Species: 446 (Legionella pneumophila) [Search protein sequence]
MGKNVVVLGTQWGDEGKGKIVDLLTQDAQVVVRYQGGHNAGHTLKITVLR
LIPSGMLRPNVTCYIANGVVLSPQALLSEIKELEGNGINVRERLRISLAC
PLILPYHIALDKARETHRGIGPAYEDKVARRALRVGDLFHRDRFANKLTE
LLDYHNFVLTQYFKQPAVDLESLLGESLQWAEELRPMVCDVSACLHEHRK
QGENILFEGASVINGAGFGPRYIDYVLGITKAYTTRVGGGPFPTELLDDV
GKRIAERGQEFGAVTGRPRRCGWFDAVLLKRSIELNSISGLCVTKLDVLD
GLEVLRIAVAYKDRDGNILSRPPLAADDFNDLLPVYEELPGWQESTADVT
VMSDLPANARAYLKRIEEILGIPIDMLSTGPERDSTITLRGPFL
3D structure
PDB6c25 Crystal structure of Adenylosuccinate synthetase from Legionella pneumophila Philadelphia 1 in complex with GDP
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D14 K17 G41 H42
Catalytic site (residue number reindexed from 1) D14 K17 G41 H42
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 GDP A G16 G18 K19 H42 K332 D334 S415 G417 P418 G16 G18 K19 H42 K295 D297 S378 G380 P381
BS02 MG A D14 G16 D14 G16
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:6c25, PDBe:6c25, PDBj:6c25
PDBsum6c25
PubMed
UniProtQ8RNM2|PURA_LEGPN Adenylosuccinate synthetase (Gene Name=purA)

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