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1QMH

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003963molecular_functionRNA-3'-phosphate cyclase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006396biological_processRNA processing
A0016874molecular_functionligase activity
B0003824molecular_functioncatalytic activity
B0003963molecular_functionRNA-3'-phosphate cyclase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006396biological_processRNA processing
B0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT A 401
ChainResidue
AGLU14
AGLY16
AGLY17
AARG21
AARG40
AARG43
AGLN51
AHIS52

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT B 401
ChainResidue
BGLY17
BARG21
BARG40
BARG43
BHIS52
BHOH2215
BHOH2216
BGLY16

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DTO B 402
ChainResidue
BGLY234
BASN235
BGLY254
BGLU255
BLYS256
BVAL258
BVAL263
BHOH2176

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 Residues2
DetailsACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:1QMH
ChainResidueDetails
AHIS309
BHIS309

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:3KGD
ChainResidueDetails
AGLN104
BASP287
BGLN288
BHIS309
APRO131
ATYR284
AASP287
AGLN288
AHIS309
BGLN104
BPRO131
BTYR284

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Details
ChainResidueDetails
AHIS309

site_idCSA2
Number of Residues1
Details
ChainResidueDetails
BHIS309

site_idMCSA1
Number of Residues2
DetailsM-CSA 882
ChainResidueDetails
AGLU14modifies pKa
AHIS309covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 882
ChainResidueDetails
BGLU14modifies pKa
BHIS309covalent catalysis

223790

PDB entries from 2024-08-14

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