Structure of PDB 1hy0 Chain B Binding Site BS01
Receptor Information
>1hy0 Chain B (length=448) Species:
8839
(Anas platyrhynchos) [
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DPIMQMLSTSISTEQRLSEVDIQASIAYAKALEKAGILTKTELEKILSGL
EKISEELSKGVIVVTQSDEDIQTANERRLKELIGDIAGKLHTGRSRNEQV
VTDLKLFMKNSLSIISTHLLQLIKTLVERAAIEIDVILPGYTHLQKAQPI
RWSQFLLSHAVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREMLR
SELEFASISLNSMDAISERDFVVEFLSVATLLLIHLSKMAEDLIIYSTSE
FGFLTLSDAFSTGSSLMPQKKNPDSLELIRSKSGRVFGRLASILMVLKGL
PSTYNKDLQEDKEAVIDVVDTLTAVLQVATGVISTLQISKENMEKALTPE
MLATDLALYLVRKGMPFRQAHTASGKAVHLAETKGIAINNLTLEDLKSIS
PLFSSDVSQVFNFVNSVEQYTALGGTAKSSVTTQIEQLRELMKKQKEQ
Ligand information
Ligand ID
SO4
InChI
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKey
QAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
[O-]S(=O)(=O)[O-]
CACTVS 3.341
[O-][S]([O-])(=O)=O
ACDLabs 10.04
[O-]S([O-])(=O)=O
Formula
O4 S
Name
SULFATE ION
ChEMBL
DrugBank
DB14546
ZINC
PDB chain
1hy0 Chain B Residue 1002 [
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Receptor-Ligand Complex Structure
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PDB
1hy0
Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
S281 M284 K287
Binding residue
(residue number reindexed from 1)
S264 M267 K270
Annotation score
1
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.
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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Biological Process
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Cellular Component
External links
PDB
RCSB:1hy0
,
PDBe:1hy0
,
PDBj:1hy0
PDBsum
1hy0
PubMed
11258884
UniProt
P24057
|ARLY1_ANAPL Delta-1 crystallin (Gene Name=ASL1)
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