1XPO
Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003723 | molecular_function | RNA binding |
A | 0004386 | molecular_function | helicase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006353 | biological_process | DNA-templated transcription termination |
A | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0042802 | molecular_function | identical protein binding |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003723 | molecular_function | RNA binding |
B | 0004386 | molecular_function | helicase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006353 | biological_process | DNA-templated transcription termination |
B | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0042802 | molecular_function | identical protein binding |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0003723 | molecular_function | RNA binding |
C | 0004386 | molecular_function | helicase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005829 | cellular_component | cytosol |
C | 0006353 | biological_process | DNA-templated transcription termination |
C | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
C | 0016020 | cellular_component | membrane |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0042802 | molecular_function | identical protein binding |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0003723 | molecular_function | RNA binding |
D | 0004386 | molecular_function | helicase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005829 | cellular_component | cytosol |
D | 0006353 | biological_process | DNA-templated transcription termination |
D | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
D | 0016020 | cellular_component | membrane |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0042802 | molecular_function | identical protein binding |
E | 0003676 | molecular_function | nucleic acid binding |
E | 0003723 | molecular_function | RNA binding |
E | 0004386 | molecular_function | helicase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005829 | cellular_component | cytosol |
E | 0006353 | biological_process | DNA-templated transcription termination |
E | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
E | 0016020 | cellular_component | membrane |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0042802 | molecular_function | identical protein binding |
F | 0003676 | molecular_function | nucleic acid binding |
F | 0003723 | molecular_function | RNA binding |
F | 0004386 | molecular_function | helicase activity |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005829 | cellular_component | cytosol |
F | 0006353 | biological_process | DNA-templated transcription termination |
F | 0008186 | molecular_function | ATP-dependent activity, acting on RNA |
F | 0016020 | cellular_component | membrane |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 1601 |
Chain | Residue |
A | THR185 |
A | ARG212 |
A | GLU215 |
A | AGS1600 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 2601 |
Chain | Residue |
B | THR185 |
B | ARG212 |
B | AGS2600 |
B | BCM2701 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 3601 |
Chain | Residue |
C | THR185 |
C | ASP265 |
C | AGS3600 |
C | BCM3701 |
C | LYS184 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 4601 |
Chain | Residue |
D | LYS184 |
D | THR185 |
D | GLU211 |
D | AGS4600 |
D | BCM4701 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG E 5601 |
Chain | Residue |
D | ARG366 |
E | THR185 |
E | ARG212 |
E | AGS5600 |
E | BCM5701 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG F 6601 |
Chain | Residue |
F | THR185 |
F | GLU215 |
F | AGS6600 |
F | BCM6701 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE AGS A 1600 |
Chain | Residue |
A | THR158 |
A | PRO180 |
A | LYS181 |
A | ALA182 |
A | GLY183 |
A | LYS184 |
A | THR185 |
A | MET186 |
A | ARG212 |
A | PHE355 |
A | MG1601 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AGS B 2600 |
Chain | Residue |
A | ARG366 |
A | LYS367 |
A | GLU369 |
B | PRO180 |
B | LYS181 |
B | ALA182 |
B | GLY183 |
B | LYS184 |
B | THR185 |
B | MET186 |
B | ARG212 |
B | PHE355 |
B | MG2601 |
B | BCM2701 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BCM B 2701 |
Chain | Residue |
A | LYS336 |
A | GLY337 |
B | PRO180 |
B | LYS184 |
B | ASP210 |
B | GLU211 |
B | ASP265 |
B | SER266 |
B | ARG269 |
B | LEU320 |
B | THR323 |
B | AGS2600 |
B | MG2601 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AGS C 3600 |
Chain | Residue |
B | ARG366 |
C | THR158 |
C | PRO180 |
C | LYS181 |
C | ALA182 |
C | GLY183 |
C | LYS184 |
C | THR185 |
C | MET186 |
C | ARG212 |
C | PHE355 |
C | MG3601 |
C | BCM3701 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BCM C 3701 |
Chain | Residue |
B | LYS336 |
B | GLY337 |
C | PRO180 |
C | LYS184 |
C | ILE209 |
C | ASP210 |
C | GLU211 |
C | ARG212 |
C | ASP265 |
C | SER266 |
C | LEU320 |
C | THR323 |
C | AGS3600 |
C | MG3601 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AGS D 4600 |
Chain | Residue |
D | THR185 |
D | MET186 |
D | ARG212 |
D | PHE355 |
D | MG4601 |
D | BCM4701 |
C | ARG366 |
D | THR158 |
D | PRO180 |
D | LYS181 |
D | ALA182 |
D | GLY183 |
D | LYS184 |
site_id | BC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BCM D 4701 |
Chain | Residue |
C | LYS336 |
C | GLY337 |
C | ARG366 |
D | PRO180 |
D | LYS184 |
D | ASP210 |
D | GLU211 |
D | ARG212 |
D | ASP265 |
D | SER266 |
D | LEU320 |
D | THR323 |
D | AGS4600 |
D | MG4601 |
site_id | BC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AGS E 5600 |
Chain | Residue |
D | ARG366 |
D | GLU369 |
E | THR158 |
E | PRO180 |
E | LYS181 |
E | ALA182 |
E | GLY183 |
E | LYS184 |
E | THR185 |
E | MET186 |
E | ARG212 |
E | PHE355 |
E | MG5601 |
E | BCM5701 |
site_id | BC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BCM E 5701 |
Chain | Residue |
D | LYS336 |
D | GLY337 |
D | ARG366 |
E | PRO180 |
E | LYS184 |
E | ASP210 |
E | GLU211 |
E | ASP265 |
E | SER266 |
E | ARG269 |
E | LEU320 |
E | THR323 |
E | AGS5600 |
E | MG5601 |
site_id | BC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AGS F 6600 |
Chain | Residue |
E | ARG366 |
F | GLU155 |
F | THR158 |
F | PRO180 |
F | LYS181 |
F | ALA182 |
F | GLY183 |
F | LYS184 |
F | THR185 |
F | MET186 |
F | ARG212 |
F | GLU215 |
F | PHE355 |
F | MG6601 |
F | BCM6701 |
site_id | BC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BCM F 6701 |
Chain | Residue |
E | LYS336 |
E | GLY337 |
E | ARG366 |
F | PRO180 |
F | LYS184 |
F | ILE209 |
F | ASP210 |
F | GLU211 |
F | ARG212 |
F | ASP265 |
F | SER266 |
F | ARG269 |
F | LEU320 |
F | THR323 |
F | AGS6600 |
F | MG6601 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000255 |
Chain | Residue | Details |
A | ASN151 | |
B | ASN151 | |
C | ASN151 | |
D | ASN151 | |
E | ASN151 | |
F | ASN151 |
site_id | SWS_FT_FI2 |
Number of Residues | 48 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU114 | |
B | ILE209 | |
B | ALA243 | |
B | VAL246 | |
C | LEU114 | |
C | ARG144 | |
C | MET147 | |
C | ILE209 | |
C | ALA243 | |
C | VAL246 | |
D | LEU114 | |
A | ARG144 | |
D | ARG144 | |
D | MET147 | |
D | ILE209 | |
D | ALA243 | |
D | VAL246 | |
E | LEU114 | |
E | ARG144 | |
E | MET147 | |
E | ILE209 | |
E | ALA243 | |
A | MET147 | |
E | VAL246 | |
F | LEU114 | |
F | ARG144 | |
F | MET147 | |
F | ILE209 | |
F | ALA243 | |
F | VAL246 | |
A | LYS181 | |
A | ARG212 | |
B | LYS181 | |
A | ILE209 | |
B | ARG212 | |
C | LYS181 | |
C | ARG212 | |
D | LYS181 | |
D | ARG212 | |
E | LYS181 | |
E | ARG212 | |
F | LYS181 | |
F | ARG212 | |
A | ALA243 | |
A | VAL246 | |
B | LEU114 | |
B | ARG144 | |
B | MET147 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY169 | |
B | GLY169 | |
C | GLY169 | |
D | GLY169 | |
E | GLY169 | |
F | GLY169 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: RNA-binding 2 |
Chain | Residue | Details |
A | LYS326 | |
B | LYS326 | |
C | LYS326 | |
D | LYS326 | |
E | LYS326 | |
F | LYS326 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
A | ARG366 |
site_id | CSA10 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
D | ARG212 | |
D | GLU211 | |
D | LYS184 |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
E | ARG212 | |
E | GLU211 | |
E | LYS184 |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
F | ARG212 | |
F | GLU211 | |
F | LYS184 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
B | ARG366 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
C | ARG366 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
D | ARG366 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
E | ARG366 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
F | ARG366 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
A | ARG212 | |
A | GLU211 | |
A | LYS184 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
B | ARG212 | |
B | GLU211 | |
B | LYS184 |
site_id | CSA9 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ohh |
Chain | Residue | Details |
C | ARG212 | |
C | GLU211 | |
C | LYS184 |