4MI4
Crystal structure of spermidine N-acetyltransferase from Vibrio cholerae in complex with spermine
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 | 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 | 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 | 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 | 14 |
| Details | BINDING SITE FOR RESIDUE SPM A 201 |
| Chain | Residue |
| A | ASN22 |
| B | ILE50 |
| B | ASP52 |
| B | GLU55 |
| B | HOH316 |
| B | HOH401 |
| A | GLU33 |
| A | GLU34 |
| A | TYR36 |
| A | GLU37 |
| A | GLU41 |
| A | HOH309 |
| A | HOH397 |
| B | HIS49 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SPM B 201 |
| Chain | Residue |
| B | ASN22 |
| B | GLU33 |
| B | TYR36 |
| B | GLU37 |
| B | GLU41 |
| B | HOH311 |
| B | HOH377 |
| C | HIS49 |
| C | ILE50 |
| C | ASP52 |
| C | GLU55 |
| C | HOH315 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SPM C 201 |
| Chain | Residue |
| A | HIS49 |
| A | ILE50 |
| A | ASP52 |
| A | GLU55 |
| A | HOH385 |
| C | ASN22 |
| C | GLU33 |
| C | TYR36 |
| C | GLU37 |
| C | GLU41 |
| C | HOH329 |
| C | HOH489 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951 |
| Chain | Residue | Details |
| A | TYR134 | |
| B | TYR134 | |
| C | TYR134 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|Ref.3, ECO:0007744|PDB:4MJ8 |
| Chain | Residue | Details |
| A | MET28 | |
| A | GLU84 | |
| B | MET28 | |
| B | GLU84 | |
| C | MET28 | |
| C | GLU84 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4 |
| Chain | Residue | Details |
| A | GLU33 | |
| B | GLU33 | |
| C | GLU33 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4, ECO:0007744|PDB:4R87 |
| Chain | Residue | Details |
| A | GLU41 | |
| B | GLU41 | |
| C | GLU41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R87 |
| Chain | Residue | Details |
| A | HIS49 | |
| B | HIS49 | |
| C | HIS49 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|PubMed:26410587, ECO:0007744|PDB:5CNP |
| Chain | Residue | Details |
| A | GLU75 | |
| B | GLU75 | |
| C | GLU75 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57, ECO:0007744|PDB:4R87 |
| Chain | Residue | Details |
| A | ILE87 | |
| A | GLN94 | |
| B | ILE87 | |
| B | GLN94 | |
| C | ILE87 | |
| C | GLN94 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57 |
| Chain | Residue | Details |
| A | ASN127 | |
| B | ASN127 | |
| C | ASN127 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | SITE: Could be important for selectivity toward long polyamines => ECO:0000305|PubMed:25623305 |
| Chain | Residue | Details |
| A | GLU84 | |
| B | GLU84 | |
| C | GLU84 |
