Structure of PDB 3kgd Chain C

Receptor sequence
>3kgdC (length=338) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence]
MKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITSIRAGRAKPGLLRQ
HLTAVKAATEICGATVEGAELGSQRLLFRPGTVRGGDYRFAIGSAGSCTL
VLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGIHQ
QTTLLRHGFYPAGGGVVATEVSPVASFNTLQLGERGNIVQMRGEVLLAGV
PRHVAEREIATLAGSFSLHEQNIHNLPRDQGPGNTVSLEVESENITERFF
VVGEKRVSAEVVAAQLVKEVKRYLASTAAVGEYLADQLVLPMALAGAGEF
TVAHPSCHLLTNIAVVERFLPVRFSLIETDGVTRVSIE
3D structure
PDB3kgd Structure of the RNA 3'-phosphate cyclase-adenylate intermediate illuminates nucleotide specificity and covalent nucleotidyl transfer.
ChainC
Resolution1.68 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 H309
Catalytic site (residue number reindexed from 1) E13 H308
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 C S129 A130 P131 F135 F251 Y284 D287 Q288 H309 S128 A129 P130 F134 F250 Y283 D286 Q287 H308
BS02 SO4 C E14 R43 E13 R42
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:3kgd, PDBe:3kgd, PDBj:3kgd
PDBsum3kgd
PubMed20399182
UniProtP46849|RTCA_ECOLI RNA 3'-terminal phosphate cyclase (Gene Name=rtcA)

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