Structure of PDB 4mx2 Chain D

Receptor sequence
>4mx2D (length=439) Species: 5661 (Leishmania donovani) [Search protein sequence]
EISQDSPLYSLSPLDGRYKRDTTPLRAYFSEYALFKYRVQVEVLYFEALC
KEVPAITQLRGVTDAQLGELRATTFENFAVDDAKIIKGIEAVTNHDIKAV
EYYLKDKMSACGLEAEKEFIHFGLTSQDINNTSIPMLLRDALHHHYIPTL
DQLIALLKSKLPEWDVPMLARTHGQPASPTNLAKEFMVWIERLEEQRTML
LSIPNTGKFGGATGNFNAHLCAYPGVNWLDFGELFLSKYLGLRRQRYTTQ
IEHYDNLAAICDACARLHTILMDLAKDVWQYISLGYFDQKVRAGEVGVNP
IDFENAEGNLGMSNAVLGFLSAKLPISRLQRDLTDSTVLRNLGVPLSHAL
IAFASLRRGIDKLLLNKDVIASDLEGNWAVVAEGIQTVLRREGYPKPYEA
LKVTEETVHRFVQQLITEEVRQELLAITPFTYVGYTAHP
3D structure
PDB4mx2 Crystal Structure of adenylosuccinate lyase from Leishmania donovani
ChainD
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) H118 T195 H196 E334
Catalytic site (residue number reindexed from 1) H95 T172 H173 E304
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 D R40 Y41 I331 N335 R17 Y18 I301 N305
BS02 AMP D N117 H118 D119 R361 L363 S366 T367 R370 N94 H95 D96 R331 L333 S336 T337 R340
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4mx2, PDBe:4mx2, PDBj:4mx2
PDBsum4mx2
PubMed
UniProtA7LBL3

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