4YGO
Dodecameric structure of spermidine N-acetyltransferase from Vibrio cholerae in intermediate state
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 |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004145 | molecular_function | diamine N-acetyltransferase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006598 | biological_process | polyamine catabolic process |
D | 0016740 | molecular_function | transferase activity |
D | 0016746 | molecular_function | acyltransferase activity |
D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
D | 0046203 | biological_process | spermidine catabolic process |
D | 0046208 | biological_process | spermine catabolic process |
D | 0046872 | molecular_function | metal ion binding |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0004145 | molecular_function | diamine N-acetyltransferase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0006598 | biological_process | polyamine catabolic process |
E | 0016740 | molecular_function | transferase activity |
E | 0016746 | molecular_function | acyltransferase activity |
E | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
E | 0046203 | biological_process | spermidine catabolic process |
E | 0046208 | biological_process | spermine catabolic process |
E | 0046872 | molecular_function | metal ion binding |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0004145 | molecular_function | diamine N-acetyltransferase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006598 | biological_process | polyamine catabolic process |
F | 0016740 | molecular_function | transferase activity |
F | 0016746 | molecular_function | acyltransferase activity |
F | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
F | 0046203 | biological_process | spermidine catabolic process |
F | 0046208 | biological_process | spermine catabolic process |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 201 |
Chain | Residue |
A | GLU33 |
A | GLU75 |
B | GLU33 |
B | GLU75 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CA A 202 |
Chain | Residue |
A | PRO35 |
A | GLU41 |
A | HOH315 |
D | ASN53 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CA B 201 |
Chain | Residue |
C | PRO35 |
C | GLU41 |
C | HOH322 |
B | ASN53 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CA D 201 |
Chain | Residue |
C | GLU33 |
C | GLU75 |
D | GLU33 |
D | GLU75 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CA D 202 |
Chain | Residue |
C | ASN53 |
C | HOH316 |
D | GLU34 |
D | PRO35 |
D | GLU41 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CA E 201 |
Chain | Residue |
E | GLU33 |
E | GLU75 |
F | GLU33 |
F | GLU75 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 785 |
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 | 6 |
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 | 18 |
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 | 6 |
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 | 6 |
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 | 18 |
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 | 6 |
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 | 48 |
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 | 54 |
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 | 6 |
Details | Site: {"description":"Could be important for selectivity toward long polyamines","evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |