Structure of PDB 2j91 Chain C

Receptor sequence
>2j91C (length=456) Species: 9606 (Homo sapiens) [Search protein sequence]
GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLG
LPITDEQIREMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAG
IIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPT
LGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGT
QASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSV
LASLGASVHKICTDIRLLANLKEMEEPYKRNPMRSERCCSLARHLMTLVM
DPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYP
KVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQ
EGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVY
PLLKPY
3D structure
PDB2j91 Crystal Structure of Human Adenylosuccinate Lyase
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H86 T158 H159 K295 E302
Catalytic site (residue number reindexed from 1) H82 T154 H155 K279 E286
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 AMP C R85 H86 D87 Q241 S334 R338 R81 H82 D83 Q237 S318 R322
BS02 AMP C R20 Y21 M299 R16 Y17 M283
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2j91, PDBe:2j91, PDBj:2j91
PDBsum2j91
PubMed
UniProtP30566|PUR8_HUMAN Adenylosuccinate lyase (Gene Name=ADSL)

[Back to BioLiP]