Structure of PDB 3vpd Chain A

Receptor sequence
>3vpdA (length=281) Species: 274 (Thermus thermophilus) [Search protein sequence]
MLAILYDRIRPDERMLFERAEALGLPYKKVYVPALPMVLGERPEALEGVT
VALERCVSQSRGLAAARYLTALGIPVVNRPEVIEACGDKWATSVALAKAG
LPQPKTALATDREEALRLMEAFGYPVVLKPVIGSWGRLLAKVTDRAAAEA
LLEHKEVLGGFQHQLFYIQEYVEKPGRDIRVFVVGERAIAAIYRRSAHWI
TNTARGGQAENCPLTEEIARLSVGAAEAVGGGVVAVDLFESERGLLVNEV
NHTMEFKNSVHTTGVDIPGEILRYAWEVARG
3D structure
PDB3vpd Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
ChainA
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.2.43: [amino-group carrier protein]--L-2-aminoadipate ligase.
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 V127 K129 W135 G136 L139 Q169 V172 K174 D178 R194 W199 T201 F239 E249 V127 K129 W135 G136 L139 Q169 V172 K174 D178 R194 W199 T201 F239 E249
BS02 BUA A F256 K257 N258 S259 F256 K257 N258 S259
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0018169 ribosomal S6-glutamic acid ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0009085 lysine biosynthetic process
GO:0009432 SOS response
GO:0018410 C-terminal protein amino acid modification
GO:0019878 lysine biosynthetic process via aminoadipic acid
GO:0036211 protein modification process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:3vpd, PDBe:3vpd, PDBj:3vpd
PDBsum3vpd
PubMed23434852
UniProtQ5SH23|LYSX_THET8 Alpha-aminoadipate--LysW ligase LysX (Gene Name=lysX)

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