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1QMI

Crystal structure of RNA 3'-terminal phosphate cyclase, an ubiquitous enzyme with unusual topology

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003963molecular_functionRNA-3'-phosphate cyclase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006396biological_processRNA processing
A0016874molecular_functionligase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003963molecular_functionRNA-3'-phosphate cyclase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006396biological_processRNA processing
B0016874molecular_functionligase activity
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003963molecular_functionRNA-3'-phosphate cyclase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006396biological_processRNA processing
C0016874molecular_functionligase activity
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0003963molecular_functionRNA-3'-phosphate cyclase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006396biological_processRNA processing
D0016874molecular_functionligase activity
Functional Information from PROSITE/UniProt
site_idPS01287
Number of Residues11
DetailsRTC RNA 3'-terminal phosphate cyclase signature. HGfyPaGGGvV
ChainResidueDetails
AHIS158-VAL168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"20399182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QMH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20399182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KGD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qmh
ChainResidueDetails
AHIS309

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qmh
ChainResidueDetails
BHIS309

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qmh
ChainResidueDetails
CHIS309

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qmh
ChainResidueDetails
DHIS309

site_idMCSA1
Number of Residues2
DetailsM-CSA 882
ChainResidueDetails
ASER22modifies pKa
AGLU329covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 882
ChainResidueDetails
BSER22modifies pKa
BGLU329covalent catalysis

site_idMCSA3
Number of Residues2
DetailsM-CSA 882
ChainResidueDetails
CSER22modifies pKa
CGLU329covalent catalysis

site_idMCSA4
Number of Residues2
DetailsM-CSA 882
ChainResidueDetails
DSER22modifies pKa
DGLU329covalent catalysis

238895

PDB entries from 2025-07-16

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