4AVC
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 | 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 | 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 | 13 |
| Details | BINDING SITE FOR RESIDUE CMP A 400 |
| Chain | Residue |
| A | ALA79 |
| A | ALA100 |
| A | VAL102 |
| A | ARG138 |
| A | PHE142 |
| A | MSE85 |
| A | VAL87 |
| A | GLY88 |
| A | GLU89 |
| A | ILE90 |
| A | ALA91 |
| A | ARG98 |
| A | SER99 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CMP B 400 |
| Chain | Residue |
| B | ARG80 |
| B | VAL87 |
| B | GLY88 |
| B | GLU89 |
| B | ILE90 |
| B | ALA91 |
| B | ARG98 |
| B | SER99 |
| B | ALA100 |
| B | ARG138 |
| B | PHE142 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ACO B 1334 |
| Chain | Residue |
| 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 | HOH2032 |
| B | HOH2043 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ACO A 1334 |
| Chain | Residue |
| A | THR180 |
| A | ARG183 |
| A | ILE236 |
| A | ALA237 |
| A | PHE238 |
| A | VAL240 |
| A | GLN245 |
| A | GLY246 |
| A | GLY248 |
| A | ILE249 |
| A | GLY250 |
| A | SER251 |
| A | ARG272 |
| A | ASN277 |
| A | PRO279 |
| A | MSE280 |
| A | THR282 |
| A | ILE283 |
| A | ARG286 |
| A | HOH2033 |
| A | HOH2034 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 1335 |
| Chain | Residue |
| A | GLU52 |
| A | PRO53 |
| B | GLU13 |
| B | VAL30 |
| B | ALA33 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 1336 |
| Chain | Residue |
| B | ILE174 |
| B | PHE176 |
| B | SER177 |
| B | LEU181 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1337 |
| Chain | Residue |
| A | ASP95 |
| B | ILE303 |
| B | ASP304 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 1335 |
| Chain | Residue |
| A | ILE86 |
| A | GLU89 |
| A | LEU131 |
| A | ARG133 |
| A | THR134 |
| A | ALA135 |
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 |
