4FT8
E. coli Catabolite Activator Protein with Cobalt and Sulfate Ligands
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003680 | molecular_function | minor groove of adenine-thymine-rich DNA binding |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0006351 | biological_process | DNA-templated transcription |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0008301 | molecular_function | DNA binding, bending |
A | 0030552 | molecular_function | cAMP binding |
A | 0032993 | cellular_component | protein-DNA complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0043565 | molecular_function | sequence-specific DNA binding |
A | 0045013 | biological_process | carbon catabolite repression of transcription |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
B | 0003677 | molecular_function | DNA binding |
B | 0003680 | molecular_function | minor groove of adenine-thymine-rich DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0006351 | biological_process | DNA-templated transcription |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0008301 | molecular_function | DNA binding, bending |
B | 0030552 | molecular_function | cAMP binding |
B | 0032993 | cellular_component | protein-DNA complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0043565 | molecular_function | sequence-specific DNA binding |
B | 0045013 | biological_process | carbon catabolite repression of transcription |
B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CMP A 301 |
Chain | Residue |
A | VAL49 |
A | THR127 |
A | HOH415 |
A | HOH417 |
A | HOH475 |
B | LEU124 |
B | SER128 |
A | LEU61 |
A | ILE70 |
A | GLY71 |
A | GLU72 |
A | LEU73 |
A | ARG82 |
A | SER83 |
A | ALA84 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | HIS21 |
A | LYS22 |
A | HOH570 |
B | LYS35 |
B | GLY79 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | HIS31 |
A | TRP85 |
A | HOH508 |
A | HOH549 |
B | HIS31 |
B | TRP85 |
B | HOH568 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 304 |
Chain | Residue |
A | GLY33 |
A | GLU81 |
A | HOH442 |
A | HOH470 |
A | HOH558 |
B | SER27 |
B | THR28 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 305 |
Chain | Residue |
A | THR168 |
A | ARG169 |
A | GLN170 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 306 |
Chain | Residue |
A | THR90 |
A | ALA91 |
A | HOH599 |
A | HOH601 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 307 |
Chain | Residue |
A | HIS19 |
A | ILE20 |
A | HOH482 |
A | HOH566 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO A 308 |
Chain | Residue |
A | HIS19 |
A | HIS21 |
A | GLU96 |
A | HOH402 |
B | GLU37 |
site_id | AC9 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE CMP B 301 |
Chain | Residue |
A | LEU124 |
A | SER128 |
B | VAL49 |
B | LEU61 |
B | SER62 |
B | ILE70 |
B | GLY71 |
B | GLU72 |
B | LEU73 |
B | ARG82 |
B | SER83 |
B | ALA84 |
B | VAL86 |
B | ARG123 |
B | THR127 |
B | HOH412 |
B | HOH416 |
B | HOH417 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 302 |
Chain | Residue |
A | LYS35 |
A | HOH478 |
A | HOH583 |
B | ILE20 |
B | HIS21 |
B | LYS22 |
B | HOH573 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 303 |
Chain | Residue |
B | ASP68 |
B | GLN119 |
B | ARG122 |
B | ARG123 |
B | HOH457 |
B | HOH460 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 304 |
Chain | Residue |
B | ASP138 |
B | VAL139 |
B | ARG142 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 305 |
Chain | Residue |
B | SER179 |
B | ARG180 |
B | HOH590 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 306 |
Chain | Residue |
B | LYS57 |
B | CYS178 |
B | SER179 |
B | THR182 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 307 |
Chain | Residue |
B | THR168 |
B | ARG169 |
B | GLN170 |
B | ARG180 |
B | HOH520 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 308 |
Chain | Residue |
B | GLY200 |
B | LYS201 |
B | HOH586 |
A | SER197 |
A | TYR206 |
B | HIS199 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO B 309 |
Chain | Residue |
A | GLU37 |
A | HOH412 |
B | HIS19 |
B | HIS21 |
B | GLU96 |
Functional Information from PROSITE/UniProt
site_id | PS00042 |
Number of Residues | 24 |
Details | HTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSreTv.GRiLkmL |
Chain | Residue | Details |
A | ILE167-LEU190 |
site_id | PS00888 |
Number of Residues | 17 |
Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG |
Chain | Residue | Details |
A | LEU29-GLY45 |
site_id | PS00889 |
Number of Residues | 19 |
Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA |
Chain | Residue | Details |
A | ILE70-ALA88 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 |
Chain | Residue | Details |
A | SER179-ARG185 | |
B | SER179-ARG185 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802 |
Chain | Residue | Details |
A | GLY56 | |
B | THR127 | |
B | ALA135 | |
B | GLN170 | |
A | GLY71 | |
A | ARG82 | |
A | THR127 | |
A | ALA135 | |
A | GLN170 | |
B | GLY56 | |
B | GLY71 | |
B | ARG82 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616 |
Chain | Residue | Details |
A | GLU96 | |
B | GLU96 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616 |
Chain | Residue | Details |
A | LYS101 | |
B | LYS101 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS100 | |
B | LYS100 |