Structure of PDB 4xfj Chain A

Receptor sequence
>4xfjA (length=395) Species: 1078020 (Mycolicibacterium thermoresistibile ATCC 19527) [Search protein sequence]
SERVILAYSGGLDTSVAISWIGKETGREVVAVAIDLGQGGEDMEVVRQRA
LDCGAVESIVIDARDEFANDYCVPAIQSNALYMDRYPLVSALSRPLIVKH
LVKAAREHGGTIVAHGCTGKGNDQVRFEVGFASLAPDLEVLAPVRDYAWT
REKAIAFAEENNIPINVTSPFSIDQNVWGRAVETGFLEHLWNAPTKDVYS
YTEDPTVNWSTPDEVIVGFEQGVPVSIDGRSVTPLQAIEELNRRGGEQGV
GRLDVVEDRLVGIKSREIYEAPGAMVLITAHTELEHVTLERELGRFKRIT
DQKWGELVYDGLWFSPLKTALESFVAKTQEHVTGEIRMVLHGGHIAVNGR
RSPKSLYDFNLATYDEGDTFDQSAAKGFVQIHGLSSSISARRDLQ
3D structure
PDB4xfj Crystal structure of Argininosuccinate synthase from Mycobacterium thermoresistibile in complex with AMPPNP and Arginine
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D14 R95 D124 S175
Catalytic site (residue number reindexed from 1) D13 R94 D123 S172
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 ANP A A8 Y9 S10 T15 I35 G117 C118 F128 A7 Y8 S9 T14 I34 G116 C117 F127
BS02 ARG A Y87 S91 R127 E186 E260 E270 Y272 Y86 S90 R126 E183 E257 E267 Y269
Gene Ontology
Molecular Function
GO:0004055 argininosuccinate synthase activity
GO:0005524 ATP binding
GO:0016874 ligase 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:4xfj, PDBe:4xfj, PDBj:4xfj
PDBsum4xfj
PubMed
UniProtG7CBN9

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