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 | 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 | 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 | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951 |
Chain | Residue | Details |
A | LYS143 | |
B | LYS143 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16210326 |
Chain | Residue | Details |
A | TYR97 | |
A | GLY106 | |
A | GLU136 | |
A | MSE145 | |
B | TYR97 | |
B | GLY106 | |
B | GLU136 | |
B | MSE145 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: May have an important role in the acetylation of the polyamine => ECO:0000305|PubMed:16210326 |
Chain | Residue | Details |
A | LYS143 | |
B | LYS143 |
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 |