Structure of PDB 2du3 Chain A

Receptor sequence
>2du3A (length=534) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
MKFDPQKYRELAEKDFEAAWKAGKEILAERSPNELYPRVGFSFGKEHPLF
ATIQRLREAYLSIGFSEVVNPLIVEDVHVKKQFGREALAVLDRCFYLATL
PKPNVGISAEKIRQIEAITKREVDSKPLQEIFHRYKKGEIDGDDLSYLIA
EVLDVDDITAVKILDEVFPEFKELKPISSTLTLRSHMTTGWFITLSHIAD
KLPLPIKLFSIDRCFRREQGEDATRLYTYFSASCVLVDEELSVDDGKAVA
EALLRQFGFENFRFRKDEKRSKYYIPDTQTEVFAFHPKLVGSSTKYSDGW
IEIATFGIYSPTALAEYDIPYPVMNLGLGVERLAMILYGYDDVRKMVYPQ
IHGEIKLSDLDIAREIKVKEVPQTAVGLKIAQSIVETAEKHASEPSPCSF
LAFEGEMMGRNVRVYVVEEEENTKLCGPAYANEVVVYKGDIYGIPKTKKW
RSFFEEGVPTGIRYIDGFAYYAARKVEEAAMREQEEVKVKARIVENLSDI
NLYIHENVRRYILWKKGKIDVRGPLFVTVKAEIE
3D structure
PDB2du3 Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.27: O-phosphoserine--tRNA 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 rna A E420 T423 P428 A429 N432 G443 R492 D520 R522 G523 P524 F526 E420 T423 P428 A429 N432 G443 R492 D520 R522 G523 P524 F526
BS02 SEP A H186 M187 T188 S231 S233 Y273 Y274 T305 N325 G327 H186 M187 T188 S231 S233 Y273 Y274 T305 N325 G327
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004826 phenylalanine-tRNA ligase activity
GO:0005524 ATP binding
GO:0042802 identical protein binding
GO:0043816 phosphoserine-tRNA(Cys) ligase activity
Biological Process
GO:0006412 translation
GO:0006432 phenylalanyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
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:2du3, PDBe:2du3, PDBj:2du3
PDBsum2du3
PubMed17351629
UniProtO30126|SEPS_ARCFU O-phosphoserine--tRNA(Cys) ligase (Gene Name=sepS)

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