Structure of PDB 1dcn Chain D

Receptor sequence
>1dcnD (length=436) Species: 8839 (Anas platyrhynchos) [Search protein sequence]
PIMEKLNSSIAYDQRLSEVDIQGSMAYAKALEKAGILTKTELEKILSGLE
KISEEWSKGVFVVKQSDEDIHTANERRLKELIGDIAGKLNTGRSRNDQVV
TDLKLFMKNSLSIISTHLLQLIKTLVERAAIEIDVILPGYTNLQKAQPIR
WSQFLLSHAVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREMLRS
ELEFASISLNSMDAISERDFVVEFLSFATLLMIHLSKMAEDLIIYSTSEF
GFLTLSDAFSTNPDSLELIRSKSGRVFGRLASILMVLKGLPSTYNKDLQE
DKEAVFDVVDTLTAVLQVATGVISTLQISKENMEKALTPEMLATDLALYL
VRKGVPFRQAHTASGKAVHLAETKGITINNLSLEDLKSISPQFSSDVSQV
FNFVNSVEQYTALAGTAKSSVTTQIEQLRELMKKQK
3D structure
PDB1dcn Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate.
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N162 E296
Catalytic site (residue number reindexed from 1) N142 E267
Enzyme Commision number 4.3.2.1: argininosuccinate 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 AS1 D R115 N116 A205 Y323 Q328 K331 R95 N96 A185 Y294 Q299 K302
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004056 argininosuccinate lyase activity
GO:0005212 structural constituent of eye lens
GO:0016829 lyase activity
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dcn, PDBe:1dcn, PDBj:1dcn
PDBsum1dcn
PubMed10029536
UniProtP24058|ARLY2_ANAPL Argininosuccinate lyase (Gene Name=ASL2)

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