Structure of PDB 1tjw Chain A

Receptor sequence
>1tjwA (length=449) Species: 8839 (Anas platyrhynchos) [Search protein sequence]
TDPIMEKLNSSIAYDQRLSEVDIQGSMAYAKALEKAGILTKTELEKILSG
LEKISEEWSKGVFVVKQSDEDIHTANERRLKELIGDIAGKLHTGRSRNDQ
VVTDLKLFMKNSLSIISTHLLQLIKTLVERAAIEIDVILPGYDHLQKAQP
IRWSQFLLSHAVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREML
RSELEFASISLNSMDAISERDFVVEFLSFATLLMIHLSKMAEDLIIYSTS
EFGFLTLSDAFSTGSSLMPQKKNPDSLELIRSKAGRVFGRLASILMVLKG
LPSTYNKDLQEDKEAVFDVVDTLTAVLQVATGVISTLQISKENMEKALTP
EMLATDLALYLVRKGVPFRQAHTASGKAVHLAETKGITINKLSLEDLKSI
SPQFSSDVSQVFNFVNSVEQYTALAGTAKSSVTTQIEQLRELMKKQKEQ
3D structure
PDB1tjw Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis
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) E88 D161 H162 S283 S284 K289 E296
Catalytic site (residue number reindexed from 1) E70 D143 H144 S265 S266 K271 E278
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 A S114 R115 N116 Y323 Q328 K331 S96 R97 N98 Y305 Q310 K313
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:1tjw, PDBe:1tjw, PDBj:1tjw
PDBsum1tjw
PubMed15320872
UniProtP24058|ARLY2_ANAPL Argininosuccinate lyase (Gene Name=ASL2)

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