Structure of PDB 1kp2 Chain A

Receptor sequence
>1kp2A (length=431) Species: 562 (Escherichia coli) [Search protein sequence]
TTILKHLPVGQRIGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEE
DYDAIPRRAMEYGAENARLIDCRKQLVAEGIAAIQCGAFHNTTGGLTYFN
TTPLGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYRYGLLTNAEL
QIYKPWLDTDFIDELGGRHEMSEFMIACGFDYEKAYSTDSNMLGATHEAK
DLEYLNSSVKIVNPIMGVKFWDESVKIPAEEVTVRFEQGHPVALNGKTFS
DDVEMMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAYE
RLLTGIHNEDTIEQYHAHGRQLGRLLYQGRWFDSQALMLRDSLQRWVASQ
ITGEVTLELRRGNDYSILNTVSENLTYKPERVFSPDDRIGQLTMRNLDIT
DTREKLFGYAKTGLLSSSAASGVPQVENLEN
3D structure
PDB1kp2 Substrate Induced Conformational Changes in Argininosuccinate Synthetase
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) D22 R106 D135 S191
Catalytic site (residue number reindexed from 1) D22 R106 D135 S187
Enzyme Commision number 6.3.4.5: argininosuccinate synthase.
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 ATP A A16 A42 D127 G128 S129 T130 D135 F139 D193 A16 A42 D127 G128 S129 T130 D135 F139 D189
Gene Ontology
Molecular Function
GO:0004055 argininosuccinate synthase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0000050 urea cycle
GO:0000053 argininosuccinate metabolic process
GO:0006526 L-arginine biosynthetic process
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:1kp2, PDBe:1kp2, PDBj:1kp2
PDBsum1kp2
PubMed11809762
UniProtP0A6E4|ASSY_ECOLI Argininosuccinate synthase (Gene Name=argG)

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