Structure of PDB 1hy0 Chain A

Receptor sequence
>1hy0A (length=447) Species: 8839 (Anas platyrhynchos) [Search protein sequence]
DPIMQMLSTSISTEQRLSEVDIQASIAYAKALEKAGILTKTELEKILSGL
EKISEELSKGVIVVTQSDEDIQTANERRLKELIGDIAGKLHTGRSRNEQV
VTDLKLFMKNSLSIISTHLLQLIKTLVERAAIEIDVILPGYTHLQKAQPI
RWSQFLLSHAVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREMLR
SELEFASISLNSMDAISERDFVVEFLSVATLLLIHLSKMAEDLIIYSTSE
FGFLTLSDAFSTGSSLMPQKKNPDSLELIRSKSGRVFGRLASILMVLKGL
PSTYNKDLQEDKEAVIDVVDTLTAVLQVATGVISTLQISKENMEKALTPE
MLATDLALYLVRKGMPFRQAHTASGKAVHLAETKGIAINNLTLEDLKSIS
PLFSSDVSQVFNFVNSVEQYTALGGTAKSSVTTQIEQLRELMKKQKE
3D structure
PDB1hy0 Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E86 T159 H160 S281 S282 K287 E294
Catalytic site (residue number reindexed from 1) E69 T142 H143 S264 S265 K270 E277
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 SO4 A S281 M284 N289 S264 M267 N272
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004056 argininosuccinate lyase activity
GO:0005212 structural constituent of eye lens
Biological Process
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1hy0, PDBe:1hy0, PDBj:1hy0
PDBsum1hy0
PubMed11258884
UniProtP24057|ARLY1_ANAPL Delta-1 crystallin (Gene Name=ASL1)

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