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 | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22773105, ECO:0007744|PDB:4AVB, ECO:0007744|PDB:4AVC |
Chain | Residue | Details |
A | GLY88 | |
A | ARG98 | |
A | ARG138 | |
B | GLY88 | |
B | ARG98 | |
B | ARG138 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:22773105 |
Chain | Residue | Details |
A | HIS173 | |
B | ARG286 | |
A | PHE238 | |
A | GLY246 | |
A | ASN277 | |
A | ARG286 | |
B | HIS173 | |
B | PHE238 | |
B | GLY246 | |
B | ASN277 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22773105 |
Chain | Residue | Details |
A | ASP214 | |
B | ASP214 |