4EV0
Crystal Structure of Thermus thermophilus Catabolite Activator Protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000976 | molecular_function | transcription cis-regulatory region binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0010628 | biological_process | positive regulation of gene expression |
| A | 0030552 | molecular_function | cAMP binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000976 | molecular_function | transcription cis-regulatory region binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0010628 | biological_process | positive regulation of gene expression |
| D | 0030552 | molecular_function | cAMP binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0043565 | molecular_function | sequence-specific DNA binding |
| D | 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 A 301 |
| Chain | Residue |
| A | PHE34 |
| A | SER86 |
| A | ALA87 |
| A | ARG126 |
| A | HOH437 |
| A | LEU53 |
| A | LEU65 |
| A | PHE74 |
| A | GLY75 |
| A | GLU76 |
| A | MET77 |
| A | SER78 |
| A | ARG85 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | SER20 |
| A | TYR21 |
| A | GLN23 |
| A | ASP104 |
| A | ARG165 |
| A | HIS167 |
| A | MG304 |
| A | HOH421 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | HIS166 |
| A | HIS167 |
| A | ARG177 |
| A | HOH416 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 304 |
| Chain | Residue |
| A | GLU103 |
| A | ASP104 |
| A | SO4302 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CMP D 301 |
| Chain | Residue |
| A | ASP131 |
| D | PHE34 |
| D | LEU65 |
| D | PHE74 |
| D | GLY75 |
| D | GLU76 |
| D | MET77 |
| D | SER78 |
| D | ARG85 |
| D | SER86 |
| D | ALA87 |
| D | ARG126 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 302 |
| Chain | Residue |
| A | ARG110 |
| D | LEU10 |
| D | GLU14 |
| D | LEU112 |
| D | PRO113 |
| D | LEU114 |
| D | HOH409 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 303 |
| Chain | Residue |
| A | ALA216 |
| D | ARG165 |
| D | HIS166 |
| D | HOH423 |
| D | HOH434 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 304 |
| Chain | Residue |
| A | ARG182 |
| D | HIS57 |
| D | LEU58 |
Functional Information from PROSITE/UniProt
| site_id | PS00889 |
| Number of Residues | 18 |
| Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEmSLldege......RSAsAvA |
| Chain | Residue | Details |
| A | PHE74-ALA91 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 132 |
| Details | Domain: {"description":"HTH crp-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00387","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 38 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00387","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 240 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00060","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2012","submissionDatabase":"PDB data bank","title":"Crystal Structure of T. thermophilius catabolite activator protein.","authors":["Hudson B.P.","Turo K.","Birktoft J.J.","Ebright R.H.","Lawson C.L."]}},{"source":"PDB","id":"4EV0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
