Structure of PDB 1k7w Chain A

Receptor sequence
>1k7wA (length=449) Species: 8839 (Anas platyrhynchos) [Search protein sequence]
TDPIMEKLNSSIAYDQRLSEVDIQGSMAYAKALEKAGILTKTELEKILSG
LEKISEEWSKGVFVVKQSDEDIHTANERRLKELIGDIAGKLHTGRSRNDQ
VVTDLKLFMKNSLSIISTHLLQLIKTLVERAAIEIDVILPGYTHLQKAQP
IRWSQFLLSHAVALTRDSERLGEVKKRINVLPLGSGALAGNPLDIDREML
RSELEFASISLNSMDAISERDFVVEFLSFATLLMIHLSKMAEDLIIYSTS
EFGFLTLSDAFSTGASLMPQKKNPDSLELIRSKAGRVFGRLASILMVLKG
LPSTYNKDLQEDKEAVFDVVDTLTAVLQVATGVISTLQISKENMEKALTP
EMLATDLALYLVRKGVPFRQAHTASGKAVHLAETKGITINKLSLEDLKSI
SPQFSSDVSQVFNFVNSVEQYTALGGTAKSSVTTQIEQLRELMKKQKEQ
3D structure
PDB1k7w Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase.
ChainA
Resolution1.96 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 T161 H162 A283 S284 K289 E296
Catalytic site (residue number reindexed from 1) E70 T143 H144 A265 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 R115 N116 Y323 Q328 K331 R97 N98 Y305 Q310 K313
BS02 AS1 A T161 H162 T143 H144
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:1k7w, PDBe:1k7w, PDBj:1k7w
PDBsum1k7w
PubMed11698398
UniProtP24058|ARLY2_ANAPL Argininosuccinate lyase (Gene Name=ASL2)

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