4I09
structure of the mutant Catabolite gene activator protein V132L
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 19 |
| Details | BINDING SITE FOR RESIDUE CMP A 301 |
| Chain | Residue |
| A | VAL50 |
| A | SER84 |
| A | ALA85 |
| A | VAL87 |
| A | ARG124 |
| A | THR128 |
| A | HOH403 |
| A | HOH409 |
| A | HOH417 |
| B | LEU125 |
| B | SER129 |
| A | LEU62 |
| A | SER63 |
| A | ILE71 |
| A | GLY72 |
| A | GLU73 |
| A | LEU74 |
| A | GLY75 |
| A | ARG83 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CMP B 301 |
| Chain | Residue |
| A | LEU125 |
| A | SER129 |
| B | VAL50 |
| B | SER63 |
| B | ILE71 |
| B | GLY72 |
| B | GLU73 |
| B | LEU74 |
| B | ARG83 |
| B | SER84 |
| B | ALA85 |
| B | VAL87 |
| B | ARG124 |
| B | THR128 |
| B | HOH401 |
| B | HOH404 |
| B | HOH452 |
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 | ILE168-LEU191 |
| site_id | PS00888 |
| Number of Residues | 17 |
| Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG |
| Chain | Residue | Details |
| A | LEU30-GLY46 |
| site_id | PS00889 |
| Number of Residues | 19 |
| Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA |
| Chain | Residue | Details |
| A | ILE71-ALA89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00387","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Region: {"description":"Activating region 2 (AR2); probably contacts the N-terminus of RpoA","evidences":[{"source":"PubMed","id":"8978616","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Region: {"description":"Activating region 3 (AR3); probably contacts sigma-70 (RpoD)","evidences":[{"source":"PubMed","id":"10860739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10860740","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Region: {"description":"Activating region 1 (AR1); probably contacts the C-terminus of RpoA","evidences":[{"source":"PubMed","id":"7966284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8392187","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 42 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11124031","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12202833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1653449","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2828639","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6286624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757802","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Activating region 2 (AR2); probably contacts the N-terminus of RpoA","evidences":[{"source":"PubMed","id":"8978616","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Activating region 2 (AR2); probably contacts the N-terminus of RpoA","evidences":[{"source":"PubMed","id":"15520470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8978616","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






