Structure of PDB 2vd6 Chain C

Receptor sequence
>2vd6C (length=457) Species: 9606 (Homo sapiens) [Search protein sequence]
GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLG
LPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAG
IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPT
LGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGT
QASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSV
LASLGASVHKICTDIRLLANLKEMEEPFYKRNPMRSERCCSLARHLMTLV
MDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVY
PKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVK
QEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEV
YPLLKPY
3D structure
PDB2vd6 Human Adenylosuccinate Lyase in Complex with its Substrate N6-(1,2-Dicarboxyethyl)-AMP, and its Products AMP and Fumarate.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H86 T158 H159 K295 E302
Catalytic site (residue number reindexed from 1) H82 T154 H155 K280 E287
Enzyme Commision number 4.3.2.2: adenylosuccinate lyase.
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 2SA C R20 Y21 K295 R303 R16 Y17 K280 R288
BS02 AMP C R85 H86 D87 Q241 R329 L331 S334 R338 R81 H82 D83 Q237 R314 L316 S319 R323
BS03 FUM C H86 S112 H82 S108
BS04 2SA C T158 H159 T154 H155
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004018 N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
GO:0016829 lyase activity
GO:0042802 identical protein binding
GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Biological Process
GO:0001666 response to hypoxia
GO:0006164 purine nucleotide biosynthetic process
GO:0006167 AMP biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0007584 response to nutrient
GO:0009060 aerobic respiration
GO:0009152 purine ribonucleotide biosynthetic process
GO:0009168 purine ribonucleoside monophosphate biosynthetic process
GO:0014850 response to muscle activity
GO:0042594 response to starvation
GO:0044208 'de novo' AMP biosynthetic process
GO:0044209 AMP salvage
GO:0097294 'de novo' XMP biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vd6, PDBe:2vd6, PDBj:2vd6
PDBsum2vd6
PubMed
UniProtP30566|PUR8_HUMAN Adenylosuccinate lyase (Gene Name=ADSL)

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