4BHP
A structural model of CAP mutant (T127L and S128I) in cGMP-bound state
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 |
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 | 6 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 |
Chain | Residue | Details |
A | SER179-ARG185 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
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 | |
A | GLY71 | |
A | ARG82 | |
A | LEU127 | |
A | ALA135 | |
A | GLN170 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616 |
Chain | Residue | Details |
A | GLU96 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS100 |