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

8PTP

Structure of Rho pentamer in complex with Rof

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
a0005515molecular_functionprotein binding
a0031554biological_processregulation of termination of DNA-templated transcription
a0031564biological_processtranscription antitermination
b0005515molecular_functionprotein binding
b0031554biological_processregulation of termination of DNA-templated transcription
b0031564biological_processtranscription antitermination
c0005515molecular_functionprotein binding
c0031554biological_processregulation of termination of DNA-templated transcription
c0031564biological_processtranscription antitermination
d0005515molecular_functionprotein binding
d0031554biological_processregulation of termination of DNA-templated transcription
d0031564biological_processtranscription antitermination
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY169
BGLY169
CGLY169
DGLY169
EGLY169

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ALYS181
EARG212
AARG212
BLYS181
BARG212
CLYS181
CARG212
DLYS181
DARG212
ELYS181

site_idSWS_FT_FI3
Number of Residues5
DetailsSITE: RNA-binding 2
ChainResidueDetails
ALYS326
BLYS326
CLYS326
DLYS326
ELYS326

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon