Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TUX

Crystal structure of RtcA.ATP.Mn ternary complex

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
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ATP A 501
ChainResidue
AGLU14
AALA130
APRO131
APHE251
ATYR284
AASP287
AGLN288
AASN309
AHOH341
AHOH380
AHOH386
AGLY16
AHOH430
AHOH567
AHOH589
AMN601
AHOH603
AHOH634
AGLY17
AGLN18
AARG21
AARG40
AARG43
AGLN104
ASER129

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 601
ChainResidue
AGLU14
AHOH392
AHOH418
AATP501

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 340
ChainResidue
ALYS45
AARG50
ASER95
AHOH414

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
ATHR35
ATHR37
AARG76
AASP88
APRO116
ASER117
AARG118

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLN104
AILE136
ALEU140
AGLN288
AHOH445
AHOH625

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AARG137
AARG137
AARG138
AHOH647
AHOH647

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
DetailsACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:1QMH
ChainResidueDetails
AASN309

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20399182, ECO:0007744|PDB:3KGD
ChainResidueDetails
AGLN104
APRO131
ATYR284
AASP287
AGLN288
AASN309

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

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon