Structure of PDB 6e5y Chain A

Receptor sequence
>6e5yA (length=438) Species: 257313 (Bordetella pertussis Tohama I) [Search protein sequence]
TTILPNLPTGQKVGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEP
DYDEIPRRAMQYGAEAARLVDCRAQLVAEGIAALQAGAFHISTAGLTYFN
TTPIGRAVTGTMLVAAMKEDGVNIWGDGSTFKGNDIERFYRYGLLTNPDL
KIYKPWLDQTFIDELGGRAEMSEYMRQAGFDYKMSAEKAYSTDSNMLGAT
HEAKDLELLSAGIRIVQPIMGVAFWQDSVQIKAEEVTVRFEEGQPVALNG
VEYADPVELLLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGLALLF
IAYERLVTGIHNEDTIEQYRENGRKLGRLLYQGRWFDPQAIMLRETAQRW
VARAITGEVTLELRRGNDYSLLNTESANLTYAPERLSMEKVENAPFTPAD
RIGQLTMRNLDIVDTREKLFTYVKTGLLAPSALPQIKD
3D structure
PDB6e5y 1.50 Angstrom Resolution Crystal Structure of Argininosuccinate Synthase from Bordetella pertussis in Complex with AMP.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D23 R107 D136 S192
Catalytic site (residue number reindexed from 1) D22 R106 D135 S191
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 AMP A A17 T42 A43 D194 A16 T41 A42 D193
Gene Ontology
Molecular Function
GO:0004055 argininosuccinate synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6e5y, PDBe:6e5y, PDBj:6e5y
PDBsum6e5y
PubMed
UniProtQ7VTJ9|ASSY_BORPE Argininosuccinate synthase (Gene Name=argG)

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