Structure of PDB 4mx2 Chain G

Receptor sequence

>4mx2G (length=427) Species: 5661 (Leishmania donovani)

EISQDSPLYSLSPLDGRYKRDTTPLRAYFSEYALFKYRVQVEVLYFEALC
KEVPAITQLRGVTDAQLGELRATTFENFAVDDAKIIKGIEAVTNHDIKAV
EYYLKDKMSACGLEAEKEFIHFGLTSQDINNTSIPMLLRDALHHHYIPTL
DQLIALLKSKLPEWDVPMLARTHGQPASPTNLAKEFMVWIERLEEQRTML
LSIPNTGKFGGATGNFNAHLCAYPGVNWLDFGELFLSKYLGLRRQRYTTQ
IEHYDNLAAICDACARLHTILMDLAKDVWQYISLGYFDQKVREVGVNPID
FENAEGNLGMSNAVLGFLSAKLPISRLQRDLTDSTVLRNLGVPLSHALIA
FASLRRGIDKLLLNKDVIASDLEGNWAVVAEGIQTVLRREGHVTEETVHR
FVQQLITEEVRQELLAITPFTYVGYTA

3D structure

• PDB: 4mx2 Crystal Structure of adenylosuccinate lyase from Leishmania donovani
• Chain: G
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H118 T195 H196 E334
• Catalytic site (residue number reindexed from 1): H95 T172 H173 E302
• 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	G	N117 H118 D119 S149 R361 L363 S366 T367 R370	N94 H95 D96 S126 R329 L331 S334 T335 R338
BS02	AMP	G	R40 Y41 I331 N335	R17 Y18 I299 N303

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:0006188 IMP biosynthetic process
• GO:0006189 'de novo' IMP biosynthetic process
• GO:0009152 purine ribonucleotide biosynthetic process
• GO:0044208 'de novo' AMP biosynthetic process

External links

• PDB: RCSB:4mx2, PDBe:4mx2, PDBj:4mx2
• PDBsum: 4mx2
• UniProt: A7LBL3