1O3T
PROTEIN-DNA RECOGNITION AND DNA DEFORMATION REVEALED IN CRYSTAL STRUCTURES OF CAP-DNA COMPLEXES
Replaces: 1DBCFunctional 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 | 13 |
| Details | BINDING SITE FOR RESIDUE CMP B 761 |
| Chain | Residue |
| A | LEU124 |
| B | SER83 |
| B | ALA84 |
| B | ARG123 |
| B | THR127 |
| A | SER128 |
| B | ILE30 |
| B | VAL49 |
| B | SER62 |
| B | GLY71 |
| B | GLU72 |
| B | LEU73 |
| B | ARG82 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CMP A 762 |
| Chain | Residue |
| A | VAL49 |
| A | LEU61 |
| A | ILE70 |
| A | GLY71 |
| A | GLU72 |
| A | LEU73 |
| A | ARG82 |
| A | SER83 |
| A | ALA84 |
| A | THR127 |
| B | LEU124 |
| B | SER128 |
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 |
