1TIQ
Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004145 | molecular_function | diamine N-acetyltransferase activity |
| A | 0004596 | molecular_function | protein-N-terminal amino-acid 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 | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0043939 | biological_process | negative regulation of sporulation |
| B | 0004145 | molecular_function | diamine N-acetyltransferase activity |
| B | 0004596 | molecular_function | protein-N-terminal amino-acid 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 | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0043939 | biological_process | negative regulation of sporulation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | PHE155 |
| B | TYR156 |
| B | HIS175 |
| B | HIS176 |
| B | HIS177 |
| B | HOH408 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE COA A 301 |
| Chain | Residue |
| A | ILE98 |
| A | GLN103 |
| A | LYS104 |
| A | LYS104 |
| A | HIS105 |
| A | GLY106 |
| A | LEU107 |
| A | GLY108 |
| A | LYS109 |
| A | ASN135 |
| A | ASN137 |
| A | ALA140 |
| A | TYR142 |
| A | LYS144 |
| A | LYS144 |
| A | COA303 |
| A | HOH1205 |
| A | HOH1220 |
| A | HOH1241 |
| A | HOH1294 |
| A | HOH1312 |
| A | HOH1321 |
| A | HOH1356 |
| A | THR27 |
| A | ILE96 |
| A | TYR97 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE COA A 303 |
| Chain | Residue |
| A | TYR40 |
| A | GLU94 |
| A | TYR97 |
| A | GLY130 |
| A | VAL131 |
| A | TRP132 |
| A | PHE155 |
| A | ASP164 |
| A | COA301 |
| A | DTT1201 |
| A | HOH1224 |
| A | HOH1363 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE COA B 302 |
| Chain | Residue |
| B | ILE96 |
| B | TYR97 |
| B | ILE98 |
| B | GLN103 |
| B | LYS104 |
| B | HIS105 |
| B | GLY106 |
| B | LEU107 |
| B | GLY108 |
| B | LYS109 |
| B | ASN135 |
| B | ASN137 |
| B | ALA138 |
| B | ALA140 |
| B | LYS144 |
| B | MSE145 |
| B | HOH403 |
| B | HOH466 |
| B | HOH467 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DTT A 1201 |
| Chain | Residue |
| A | PHE24 |
| A | ASN32 |
| A | ASN36 |
| A | MSE37 |
| A | MSE157 |
| A | GLY158 |
| A | COA303 |
| A | HOH1343 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DTT A 1202 |
| Chain | Residue |
| A | GLU22 |
| A | LYS99 |
| B | GLN18 |
| B | GLU22 |
| B | LYS99 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A951","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16210326","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"May have an important role in the acetylation of the polyamine","evidences":[{"source":"PubMed","id":"16210326","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| A | GLU92 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| B | GLU92 |
