Structure of PDB 3kgd Chain D

Receptor sequence
>3kgdD (length=340) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence]
RHMKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITSIRAGRAKPGLL
RQHLTAVKAATEICGATVEGAELGSQRLLFRPGTVRGGDYRFAIGSAGSC
TLVLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGI
HQQTTLLRHGFYPAGGGVVATEVSPVASFNTLQLGERGNIVQMRGEVLLA
GVPRHVAEREIATLAGSFSLHEQNIHNLPRDQGPGNTVSLEVESENITER
FFVVGEKRVSAEVVAAQLVKEVKRYLASTAAVGEYLADQLVLPMALAGAG
EFTVAHPSCHLLTNIAVVERFLPVRFSLIETDGVTRVSIE
3D structure
PDB3kgd Structure of the RNA 3'-phosphate cyclase-adenylate intermediate illuminates nucleotide specificity and covalent nucleotidyl transfer.
ChainD
Resolution1.68 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E14 H309
Catalytic site (residue number reindexed from 1) E15 H310
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 AMP D S129 A130 P131 F135 F251 Y284 D287 Q288 H309 S130 A131 P132 F136 F252 Y285 D288 Q289 H310
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3kgd, PDBe:3kgd, PDBj:3kgd
PDBsum3kgd
PubMed20399182
UniProtP46849|RTCA_ECOLI RNA 3'-terminal phosphate cyclase (Gene Name=rtcA)

[Back to BioLiP]