Structure of PDB 4efc Chain A

Receptor sequence
>4efcA (length=452) [Search protein sequence]
VDYSVDNPLFALSPLDGRYKRQTKALRAFFSEYGFFRYRVLVEVEYFTAL
CKDVPTIVPLRSVTDEQLQKLRKITLDCFSVSSAEEIKRLERVTNHDIKA
VEYFIKERMDTCGLSHVTEFVHFGLTSQDINNTAIPMMIRDAIVTLYLPA
LDGIIGSLTSKLVDWDVPMLARTHGQPASPTNLAKEFVVWIERLREQRRQ
LCEVPTTGKFGGATGNFNAHLVAYPSVNWRAFADMFLAKYLGLKRQQATT
QIENYDHLAALCDACARLHVILIDMCRDVWQYISMGFFKQKVKEGEVGSS
TMPHKVNPIDFENAEGNLALSNALLNFFASKLPISRLQRDLTDSTVLRNL
GVPIGHACVAFASISQGLEKLMISRETISRELSSNWAVVAEGIQTVLRRE
CYPKPYETLKKLTVTEEQVRNFINGLTDISDDVRAELLAITPFTYVGYVP
RF
3D structure
PDB4efc Crystal Structure of Adenylosuccinate Lyase from Trypanosoma Brucei, Tb427tmp.160.5560
ChainA
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) H107 T184 H185 S311 K316 E323
Catalytic site (residue number reindexed from 1) H96 T173 H174 S300 K305 E312
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 N106 H107 D108 S138 Q139 R350 L352 S355 T356 R359 N95 H96 D97 S127 Q128 R339 L341 S344 T345 R348
BS02 MG A D285 D289 D274 D278
BS03 AMP A R29 Y30 I320 N324 R18 Y19 I309 N313
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:0046872 metal ion binding
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
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4efc, PDBe:4efc, PDBj:4efc
PDBsum4efc
PubMed
UniProtQ38EJ2

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