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 | 38 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 |
Chain | Residue | Details |
A | HIS166-HIS185 | |
D | HIS166-HIS185 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00060 |
Chain | Residue | Details |
A | LEU6 | |
D | LEU6 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0007744|PDB:4EV0 |
Chain | Residue | Details |
A | GLY75 | |
A | ARG85 | |
D | GLY75 | |
D | ARG85 |