Structure of PDB 1tj7 Chain B

Receptor sequence
>1tj7B (length=451) Species: 562 (Escherichia coli) [Search protein sequence]
RFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQA
QLEEALNVLLEDVRARPQQILESDAEDIHSWVEGKLIDKVGQLGKKLHTG
RSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTH
LQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYE
IDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDL
IFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGM
MMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRC
QEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLP
LSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARL
G
3D structure
PDB1tj7 Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli.
ChainB
Resolution2.44 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H156 S277 K283 E290
Catalytic site (residue number reindexed from 1) H150 S271 K277 E284
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 PO4 B S277 M280 K283 S271 M274 K277
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004056 argininosuccinate lyase activity
GO:0016829 lyase activity
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
GO:0005737 cytoplasm
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:1tj7, PDBe:1tj7, PDBj:1tj7
PDBsum1tj7
PubMed15502303
UniProtP11447|ARLY_ECOLI Argininosuccinate lyase (Gene Name=argH)

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