1OJL
Crystal structure of a sigma54-activator suggests the mechanism for the conformational switch necessary for sigma54 binding
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0008134 | molecular_function | transcription factor binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0043565 | molecular_function | sequence-specific DNA binding |
B | 0005524 | molecular_function | ATP binding |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0008134 | molecular_function | transcription factor binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0043565 | molecular_function | sequence-specific DNA binding |
C | 0005524 | molecular_function | ATP binding |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0008134 | molecular_function | transcription factor binding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0043565 | molecular_function | sequence-specific DNA binding |
D | 0005524 | molecular_function | ATP binding |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0008134 | molecular_function | transcription factor binding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0043565 | molecular_function | sequence-specific DNA binding |
E | 0005524 | molecular_function | ATP binding |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0008134 | molecular_function | transcription factor binding |
E | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0043565 | molecular_function | sequence-specific DNA binding |
F | 0005524 | molecular_function | ATP binding |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0008134 | molecular_function | transcription factor binding |
F | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A1442 |
Chain | Residue |
A | SER171 |
A | GLY172 |
A | THR173 |
A | LYS175 |
A | ARG359 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B1390 |
Chain | Residue |
B | ARG359 |
B | SER171 |
B | GLY172 |
B | THR173 |
B | LYS175 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 C1391 |
Chain | Residue |
C | ASP170 |
C | SER171 |
C | GLY172 |
C | THR173 |
C | LYS175 |
C | ARG359 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 D1442 |
Chain | Residue |
D | SER171 |
D | GLY172 |
D | THR173 |
D | LYS175 |
D | ARG359 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 F1390 |
Chain | Residue |
F | SER171 |
F | GLY172 |
F | THR173 |
F | LYS175 |
F | GLU176 |
F | ASP240 |
F | ARG359 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ATP E1442 |
Chain | Residue |
E | ILE142 |
E | SER171 |
E | GLY172 |
E | THR173 |
E | GLY174 |
E | LYS175 |
E | GLU176 |
E | ASP240 |
E | ARG315 |
E | LEU322 |
E | PHE326 |
E | ARG329 |
E | ILE358 |
E | ARG359 |
E | GLU362 |
Functional Information from PROSITE/UniProt
site_id | PS00675 |
Number of Residues | 14 |
Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLIhGDSGTGKelV |
Chain | Residue | Details |
A | VAL165-VAL178 |
site_id | PS00676 |
Number of Residues | 16 |
Details | SIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GrFveADGGTLFLDEI |
Chain | Residue | Details |
A | GLY227-ILE242 |
site_id | PS00688 |
Number of Residues | 10 |
Details | SIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNIRELeN |
Chain | Residue | Details |
A | TRP354-ASN363 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 114 |
Details | DNA_BIND: H-T-H motif => ECO:0000250 |
Chain | Residue | Details |
A | LYS421-SER440 | |
B | LYS421-SER440 | |
C | LYS421-SER440 | |
D | LYS421-SER440 | |
E | LYS421-SER440 | |
F | LYS421-SER440 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16005641, ECO:0007744|PDB:1OJL |
Chain | Residue | Details |
A | GLY172 | |
C | THR173 | |
C | ARG329 | |
C | ARG359 | |
D | GLY172 | |
D | THR173 | |
D | ARG329 | |
D | ARG359 | |
E | GLY172 | |
E | THR173 | |
E | ARG329 | |
A | THR173 | |
E | ARG359 | |
F | GLY172 | |
F | THR173 | |
F | ARG329 | |
F | ARG359 | |
A | ARG329 | |
A | ARG359 | |
B | GLY172 | |
B | THR173 | |
B | ARG329 | |
B | ARG359 | |
C | GLY172 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8p |
Chain | Residue | Details |
A | ARG380 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8p |
Chain | Residue | Details |
B | ARG380 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8p |
Chain | Residue | Details |
C | ARG380 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8p |
Chain | Residue | Details |
D | ARG380 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8p |
Chain | Residue | Details |
E | ARG380 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8p |
Chain | Residue | Details |
F | ARG380 |