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1PV4

X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0004386molecular_functionhelicase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006353biological_processDNA-templated transcription termination
A0008186molecular_functionATP-dependent activity, acting on RNA
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0042802molecular_functionidentical protein binding
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0004386molecular_functionhelicase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006353biological_processDNA-templated transcription termination
B0008186molecular_functionATP-dependent activity, acting on RNA
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0042802molecular_functionidentical protein binding
C0003676molecular_functionnucleic acid binding
C0003723molecular_functionRNA binding
C0004386molecular_functionhelicase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006353biological_processDNA-templated transcription termination
C0008186molecular_functionATP-dependent activity, acting on RNA
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
C0042802molecular_functionidentical protein binding
D0003676molecular_functionnucleic acid binding
D0003723molecular_functionRNA binding
D0004386molecular_functionhelicase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006353biological_processDNA-templated transcription termination
D0008186molecular_functionATP-dependent activity, acting on RNA
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0042802molecular_functionidentical protein binding
E0003676molecular_functionnucleic acid binding
E0003723molecular_functionRNA binding
E0004386molecular_functionhelicase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005829cellular_componentcytosol
E0006353biological_processDNA-templated transcription termination
E0008186molecular_functionATP-dependent activity, acting on RNA
E0016020cellular_componentmembrane
E0016787molecular_functionhydrolase activity
E0016887molecular_functionATP hydrolysis activity
E0042802molecular_functionidentical protein binding
F0003676molecular_functionnucleic acid binding
F0003723molecular_functionRNA binding
F0004386molecular_functionhelicase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005829cellular_componentcytosol
F0006353biological_processDNA-templated transcription termination
F0008186molecular_functionATP-dependent activity, acting on RNA
F0016020cellular_componentmembrane
F0016787molecular_functionhydrolase activity
F0016887molecular_functionATP hydrolysis activity
F0042802molecular_functionidentical protein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY169
BGLY169
CGLY169
DGLY169
EGLY169
FGLY169

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ALYS181
EARG212
FLYS181
FARG212
AARG212
BLYS181
BARG212
CLYS181
CARG212
DLYS181
DARG212
ELYS181

site_idSWS_FT_FI3
Number of Residues6
DetailsSITE: RNA-binding 2
ChainResidueDetails
ALYS326
BLYS326
CLYS326
DLYS326
ELYS326
FLYS326

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG366

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BARG366

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
CARG366

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
DARG366

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
EARG366

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG212
AGLU211
ALYS184

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BARG212
BGLU211
BLYS184

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
CARG212
CGLU211
CLYS184

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
DARG212
DGLU211
DLYS184

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
EARG212
EGLU211
ELYS184

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
FARG366

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
FARG212
FGLU211
FLYS184

219140

PDB entries from 2024-05-01

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