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3TW3

Crystal structure of RtcA.ATP.Co ternary complex

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
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP A 401
ChainResidue
AGLU14
APRO131
APHE251
ATYR284
AASP287
AGLN288
AASN309
AHOH370
AHOH371
AHOH377
AHOH423
AGLY16
ACO501
AGLY17
AGLN18
AARG21
AARG40
AARG43
AGLN104
ASER129

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 501
ChainResidue
AGLU14
AHOH370
AATP401
AHOH423

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CO A 340
ChainResidue
AHIS225
AHIS225

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CO A 341
ChainResidue
AHIS158
AGLU221

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 342
ChainResidue
ALYS45
AARG50
ASER95
AHOH379

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 Residues1
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 Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20399182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KGD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 882
ChainResidueDetails
AGLU14modifies pKa
AASN309covalent catalysis

243911

PDB entries from 2025-10-29

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