4MJ8
Crystal structure of spermidine N-acetyltransferase from Vibrio cholerae in complex with polyamine
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 | 15 |
Details | BINDING SITE FOR RESIDUE SPM A 201 |
Chain | Residue |
A | ASN22 |
A | HOH329 |
B | HIS49 |
B | ILE50 |
B | ASP52 |
B | GLU55 |
B | HOH361 |
A | MET28 |
A | GLU33 |
A | GLU34 |
A | TYR36 |
A | GLU37 |
A | GLU41 |
A | HOH302 |
A | HOH326 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SPM A 202 |
Chain | Residue |
A | TYR30 |
A | TRP31 |
A | GLU33 |
A | GLU84 |
A | PHE85 |
A | GLN86 |
A | ILE87 |
A | LEU121 |
A | HIS122 |
A | HOH381 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EOH A 203 |
Chain | Residue |
A | HOH308 |
C | SER172 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EOH A 204 |
Chain | Residue |
A | LYS48 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SPM B 201 |
Chain | Residue |
B | ASN22 |
B | MET28 |
B | GLU33 |
B | GLU34 |
B | TYR36 |
B | GLU41 |
B | HOH301 |
B | HOH351 |
B | HOH404 |
C | HIS49 |
C | ILE50 |
C | ASP52 |
C | GLU55 |
C | HOH302 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EOH B 202 |
Chain | Residue |
B | LYS48 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE SPM C 201 |
Chain | Residue |
A | HIS49 |
A | ILE50 |
A | ASP52 |
A | GLU55 |
A | HOH341 |
A | HOH347 |
C | ASN22 |
C | MET28 |
C | GLU33 |
C | GLU34 |
C | TYR36 |
C | GLU37 |
C | GLU41 |
C | HOH303 |
C | HOH394 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EOH C 202 |
Chain | Residue |
C | TRP31 |
C | GLN86 |
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 |