4NCZ
Spermidine N-acetyltransferase from Vibrio cholerae in complex with 2-[n-cyclohexylamino]ethane sulfonate.
Replaces: 4K4LFunctional 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 | 6 |
| Details | BINDING SITE FOR RESIDUE NHE A 301 |
| Chain | Residue |
| A | ARG25 |
| A | ASN26 |
| A | ILE27 |
| A | HIS122 |
| A | ALA124 |
| A | HOH432 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| C | TYR30 |
| C | PRO35 |
| A | ASN77 |
| A | TYR78 |
| A | ILE79 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 303 |
| Chain | Residue |
| A | GLU33 |
| A | GLU75 |
| C | GLU33 |
| C | GLU75 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 304 |
| Chain | Residue |
| A | ASP52 |
| A | GLU55 |
| A | HOH445 |
| A | HOH469 |
| A | HOH472 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NHE B 301 |
| Chain | Residue |
| B | ARG25 |
| B | ASN26 |
| B | ILE27 |
| B | GLN86 |
| B | HIS122 |
| B | ILE151 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | GLY95 |
| B | LYS96 |
| B | GLY97 |
| B | PHE98 |
| B | ALA99 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| B | TYR30 |
| B | ASN77 |
| B | TYR78 |
| B | ILE79 |
| B | HOH403 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 304 |
| Chain | Residue |
| B | GLU33 |
| B | GLU33 |
| B | GLU75 |
| B | GLU75 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 305 |
| Chain | Residue |
| B | ASP52 |
| B | GLU55 |
| B | HOH444 |
| B | HOH445 |
| B | HOH446 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NHE C 301 |
| Chain | Residue |
| C | ARG25 |
| C | ASN26 |
| C | ALA124 |
| C | PHE149 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| C | GLY95 |
| C | LYS96 |
| C | GLY97 |
| C | PHE98 |
| C | ALA99 |
| C | ARG100 |
| C | HOH487 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 303 |
| Chain | Residue |
| C | ASP52 |
| C | GLU55 |
| C | HOH443 |
| C | HOH444 |
| C | HOH446 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| 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_FI3 |
| 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_FI4 |
| 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_FI5 |
| 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_FI6 |
| 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_FI7 |
| 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_FI8 |
| 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_FI9 |
| 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 |
