Structure of PDB 4eei Chain A

Receptor sequence

>4eeiA (length=414) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4)

MIKRYDVAEISKIWADENKYAKMLEVELAILEALEDRMVPKGTAAEIRAR
AQIRPERVDEIEKVTKHDIIAFCTSIAEQFTAETGKFFHFGVTSSDIIDS
ALSLQIRDSMSYVIKDLEALCDSLLTKAEETKEIITMGRSHGMFAEPMSF
GQKFLGAYVEFKRRLKDLKDFQKDGLTVQFSGAVGNYCILTTEDEKKAAD
ILGLPVEEVSTQVIPRDRIAKLISIHGLIASAIERLAVEIRHLHRSDVFE
VYEGFKKNPISTENLTGMARMLRSHVSIALENCVLWHERDISHSSAERFY
LPDNFGIMVYALRRMKNTIDNLVVQRDIIEDRVRSTSAYLSSFYLHFLVA
NTPFMREDCYKIVQQVESFSKKLQKVMHDEHNIILDIPEMDFEGIKKTYL
KEIDHVFDRSVKAR

3D structure

• PDB: 4eei Crystal Structure of Adenylosuccinate Lyase from Francisella tularensis Complexed with AMP and Succinate
• Chain: A
• Resolution: 1.921 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H67 S140 H141 K268 E275
• Catalytic site (residue number reindexed from 1): H67 S140 H141 K256 E263
• 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	A	K66 H67 D68 Q212 R301 I303 S306 R310	K66 H67 D68 Q212 R289 I291 S294 R298

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003824 catalytic activity
• GO:0004018 N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
• GO:0016829 lyase activity
• GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006189 'de novo' IMP biosynthetic process
• GO:0009152 purine ribonucleotide biosynthetic process
• GO:0044208 'de novo' AMP biosynthetic process
• GO:0044281 small molecule metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4eei, PDBe:4eei, PDBj:4eei
• PDBsum: 4eei
• UniProt: Q5NIQ1