5UG4
Structure of spermidine N-acetyltransferase SpeG from Vibrio cholerae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004145 | molecular_function | diamine N-acetyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006598 | biological_process | polyamine catabolic process |
| 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 | 0046203 | biological_process | spermidine catabolic process |
| A | 0046208 | biological_process | spermine catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004145 | molecular_function | diamine N-acetyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006598 | biological_process | polyamine catabolic process |
| 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 | 0046203 | biological_process | spermidine catabolic process |
| B | 0046208 | biological_process | spermine catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004145 | molecular_function | diamine N-acetyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006598 | biological_process | polyamine catabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0046203 | biological_process | spermidine catabolic process |
| C | 0046208 | biological_process | spermine catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 201 |
| Chain | Residue |
| A | GLU33 |
| A | GLU75 |
| A | HOH362 |
| C | GLU75 |
| C | CA201 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 202 |
| Chain | Residue |
| B | HOH329 |
| B | HOH361 |
| A | GLU34 |
| A | PRO35 |
| A | GLU41 |
| B | ASN53 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 203 |
| Chain | Residue |
| A | ASN22 |
| A | HOH306 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MRD A 204 |
| Chain | Residue |
| A | HIS122 |
| A | VAL123 |
| A | ALA124 |
| A | HOH376 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 201 |
| Chain | Residue |
| B | GLU33 |
| B | GLU33 |
| B | GLU75 |
| B | GLU75 |
| B | HOH302 |
| B | HOH302 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 202 |
| Chain | Residue |
| B | GLU33 |
| B | GLU75 |
| B | GLU75 |
| B | CA203 |
| B | HOH364 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 203 |
| Chain | Residue |
| B | GLU33 |
| B | GLU75 |
| B | GLU75 |
| B | CA202 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 204 |
| Chain | Residue |
| B | GLU34 |
| B | PRO35 |
| B | GLU41 |
| C | ASN53 |
| C | HOH304 |
| C | HOH328 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue ACT B 205 |
| Chain | Residue |
| B | ILE151 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue EOH B 206 |
| Chain | Residue |
| B | ASN53 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue CA C 201 |
| Chain | Residue |
| A | GLU33 |
| A | GLU75 |
| A | CA201 |
| A | HOH344 |
| C | GLU33 |
| C | GLU75 |
| C | CA202 |
| C | HOH306 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 202 |
| Chain | Residue |
| A | GLU75 |
| A | HOH316 |
| C | GLU33 |
| C | GLU75 |
| C | CA201 |
| C | HOH346 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 203 |
| Chain | Residue |
| A | ASN53 |
| A | HOH317 |
| A | HOH364 |
| C | GLU34 |
| C | PRO35 |
| C | GLU41 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue ACT C 204 |
| Chain | Residue |
| C | ILE151 |
| C | HOH353 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 471 |
| 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 | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A951","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine N-acetyltransferase from Vibrio cholerae in complex with polyamine.","authors":["Filippova E.V.","Minasov G.","Shuvalova L.","Kiryukhina O.","Kuhn M.L.","Anderson W.F."]}},{"source":"PDB","id":"4MJ8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MI4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MI4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26410587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CNP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R57","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Site: {"description":"Could be important for selectivity toward long polyamines","evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
