Structure of PDB 3tw3 Chain A

Receptor sequence
>3tw3A (length=336) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
RMIALDGAQGEGGGQILRSALSLSMITGQPFTITSIRAGRAKPGLLRQHL
TAVKAATEICGATVEGAELGSQRLLFRPGTVRGGDYRFAIGSAGSCTLVL
QTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGIHQQT
TLLRHGFYPAGGGVVATEVSPVASFNTLQLGERGNIVQMRGEVLLAGVPR
HVAEREIATLAGSFSLHEQNIHNLPRDQGPGNTVSLEVESENITERFFVV
GEKRVSAEVVAAQLVKEVKRYLASTAAVGEYLADQLVLPMALAGAGEFTV
AHPSSNLLTNIAVVERFLPVRFSLIETDGVTRVSIE
3D structure
PDB3tw3 Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E14 N309
Catalytic site (residue number reindexed from 1) E11 N306
Enzyme Commision number 6.5.1.4: RNA 3'-terminal-phosphate cyclase (ATP).
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 E14 G16 G17 Q18 R21 R40 R43 S129 A130 P131 F135 F251 Y284 D287 Q288 E11 G13 G14 Q15 R18 R37 R40 S126 A127 P128 F132 F248 Y281 D284 Q285
BS02 CO A E14 R43 E11 R40
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003963 RNA-3'-phosphate cyclase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006396 RNA processing
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:3tw3, PDBe:3tw3, PDBj:3tw3
PDBsum3tw3
PubMed22167800
UniProtP46849|RTCA_ECOLI RNA 3'-terminal phosphate cyclase (Gene Name=rtcA)

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