4AVB
Crystal structure of protein lysine acetyltransferase Rv0998 in complex with acetyl CoA and cAMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0016407 | molecular_function | acetyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0030552 | molecular_function | cAMP binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0016407 | molecular_function | acetyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0030552 | molecular_function | cAMP binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CMP A 400 |
| Chain | Residue |
| A | VAL67 |
| A | SER99 |
| A | ALA100 |
| A | VAL102 |
| A | ARG138 |
| A | PHE142 |
| A | HOH2091 |
| A | HOH2269 |
| A | HOH2270 |
| A | ALA79 |
| A | ARG80 |
| A | VAL87 |
| A | GLY88 |
| A | GLU89 |
| A | ILE90 |
| A | ALA91 |
| A | ARG98 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1333 |
| Chain | Residue |
| A | VAL70 |
| A | HOH2047 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1334 |
| Chain | Residue |
| A | LEU274 |
| A | SER275 |
| A | ASP276 |
| A | GLY297 |
| A | HOH2180 |
| A | HOH2242 |
| B | ARG80 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1335 |
| Chain | Residue |
| A | GLU52 |
| A | PRO53 |
| A | VAL55 |
| B | VAL12 |
| B | ARG315 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1336 |
| Chain | Residue |
| A | ASP19 |
| A | GLN22 |
| A | THR134 |
| A | HOH2006 |
| A | HOH2124 |
| A | HOH2272 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 1337 |
| Chain | Residue |
| A | PRO145 |
| A | MET157 |
| A | ARG159 |
| A | THR213 |
| A | GLY215 |
| B | PEG1337 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ACO A 1338 |
| Chain | Residue |
| A | THR180 |
| A | ARG183 |
| A | ILE236 |
| A | ALA237 |
| A | PHE238 |
| A | THR239 |
| A | VAL240 |
| A | GLN245 |
| A | GLY246 |
| A | ARG247 |
| A | GLY248 |
| A | ILE249 |
| A | GLY250 |
| A | SER251 |
| A | ARG272 |
| A | MET273 |
| A | ASN277 |
| A | VAL278 |
| A | PRO279 |
| A | THR282 |
| A | ILE283 |
| A | ARG286 |
| A | HOH2224 |
| A | HOH2226 |
| A | HOH2227 |
| A | HOH2273 |
| B | ARG286 |
| B | ACO1342 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CMP B 400 |
| Chain | Residue |
| B | VAL67 |
| B | ALA79 |
| B | ARG80 |
| B | VAL87 |
| B | GLY88 |
| B | GLU89 |
| B | ILE90 |
| B | ALA91 |
| B | ARG98 |
| B | SER99 |
| B | ALA100 |
| B | VAL102 |
| B | ARG138 |
| B | PHE142 |
| B | EDO1336 |
| B | HOH2067 |
| B | HOH2072 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1333 |
| Chain | Residue |
| B | HIS173 |
| B | ILE174 |
| B | GLN175 |
| B | ALA241 |
| B | ASP242 |
| B | ALA243 |
| B | HOH2214 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1334 |
| Chain | Residue |
| B | ARG94 |
| B | GLN327 |
| B | HOH2103 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1335 |
| Chain | Residue |
| B | GLU129 |
| B | ARG130 |
| B | ARG133 |
| B | GLY126 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1336 |
| Chain | Residue |
| B | GLN137 |
| B | ARG138 |
| B | PRO163 |
| B | CMP400 |
| B | HOH2097 |
| B | HOH2100 |
| B | HOH2102 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 1337 |
| Chain | Residue |
| A | GLY215 |
| A | PEG1337 |
| A | HOH2211 |
| B | VAL190 |
| B | SER192 |
| B | PRO193 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG B 1338 |
| Chain | Residue |
| B | ARG133 |
| B | GLN137 |
| B | GLU201 |
| B | HOH2094 |
| B | HOH2096 |
| B | HOH2101 |
| B | HOH2161 |
| B | HOH2217 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 1339 |
| Chain | Residue |
| B | TYR287 |
| B | MET302 |
| B | ILE303 |
| B | ASP304 |
| B | PRO306 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEG B 1340 |
| Chain | Residue |
| B | ARG184 |
| B | GLU235 |
| B | ILE236 |
| B | ALA270 |
| B | ALA271 |
| B | ARG272 |
| B | ACT1341 |
| B | ACO1342 |
| B | HOH2142 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 1341 |
| Chain | Residue |
| B | ARG223 |
| B | GLU235 |
| B | PEG1340 |
| B | HOH2146 |
| B | HOH2159 |
| site_id | BC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ACO B 1342 |
| Chain | Residue |
| A | THR282 |
| A | ARG286 |
| A | ACO1338 |
| B | THR180 |
| B | ARG183 |
| B | ILE236 |
| B | ALA237 |
| B | PHE238 |
| B | THR239 |
| B | VAL240 |
| B | GLN245 |
| B | GLY246 |
| B | ARG247 |
| B | GLY248 |
| B | ILE249 |
| B | GLY250 |
| B | SER251 |
| B | ARG272 |
| B | ASN277 |
| B | VAL278 |
| B | PRO279 |
| B | THR282 |
| B | ARG286 |
| B | PEG1340 |
| B | HOH2177 |
| B | HOH2179 |
| B | HOH2180 |
| B | HOH2194 |
Functional Information from PROSITE/UniProt
| site_id | PS00889 |
| Number of Residues | 18 |
| Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. VGEiALlrdsp......RSAtVtT |
| Chain | Residue | Details |
| A | VAL87-THR104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 324 |
| Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22773105","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AVB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AVC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22773105","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22773105","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
