6E1X
Crystal structure of product-bound complex of spermidine/spermine N-acetyltransferase SpeG
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 | 15 |
| Details | binding site for residue SPM A 201 |
| Chain | Residue |
| A | ASN22 |
| A | HOH383 |
| A | HOH405 |
| E | HIS49 |
| E | ILE50 |
| E | ASP52 |
| E | GLU55 |
| A | MET28 |
| A | GLU33 |
| A | TYR36 |
| A | GLU41 |
| A | HOH305 |
| A | HOH312 |
| A | HOH342 |
| A | HOH361 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue SP5 A 202 |
| Chain | Residue |
| A | TYR30 |
| A | TRP31 |
| A | PHE85 |
| A | GLN86 |
| A | ILE87 |
| A | HIS122 |
| A | TYR134 |
| A | GLU148 |
| A | PHE149 |
| A | HOH303 |
| A | HOH379 |
| A | HOH398 |
| A | HOH478 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MRD A 203 |
| Chain | Residue |
| A | TYR30 |
| A | ILE88 |
| A | ILE89 |
| A | GLN94 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue TRS A 204 |
| Chain | Residue |
| A | ASN53 |
| A | ARG56 |
| A | ILE76 |
| A | TYR78 |
| A | HOH307 |
| A | HOH434 |
| D | TYR78 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue SPM B 201 |
| Chain | Residue |
| B | ASN22 |
| B | MET28 |
| B | GLU33 |
| B | TYR36 |
| B | GLU41 |
| B | HOH305 |
| B | HOH312 |
| B | HOH344 |
| B | HOH363 |
| B | HOH399 |
| F | HIS49 |
| F | ILE50 |
| F | ASP52 |
| F | GLU55 |
| F | HOH204 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue SP5 B 202 |
| Chain | Residue |
| B | TYR30 |
| B | TRP31 |
| B | GLU75 |
| B | GLU84 |
| B | PHE85 |
| B | GLN86 |
| B | ILE87 |
| B | HIS122 |
| B | TYR134 |
| B | GLU148 |
| B | PHE149 |
| B | HOH307 |
| B | HOH316 |
| B | HOH360 |
| B | HOH374 |
| B | HOH376 |
| B | HOH449 |
| B | HOH539 |
| F | HOH409 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 203 |
| Chain | Residue |
| B | TYR30 |
| B | ILE88 |
| B | ILE89 |
| B | GLN94 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue TRS B 204 |
| Chain | Residue |
| B | ASN53 |
| B | ARG56 |
| B | ILE76 |
| B | TYR78 |
| B | HOH306 |
| B | HOH361 |
| B | HOH404 |
| C | TYR78 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue SPM C 201 |
| Chain | Residue |
| C | HOH395 |
| B | HIS49 |
| B | ILE50 |
| B | ASP52 |
| B | GLU55 |
| B | HOH311 |
| C | ASN22 |
| C | MET28 |
| C | GLU33 |
| C | TYR36 |
| C | GLU41 |
| C | HOH301 |
| C | HOH313 |
| C | HOH326 |
| C | HOH327 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue SPM C 202 |
| Chain | Residue |
| B | TYR78 |
| C | HIS49 |
| C | ILE50 |
| C | ASP52 |
| C | GLU55 |
| C | HOH304 |
| C | HOH337 |
| C | HOH467 |
| F | GLU34 |
| F | GLU41 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue HLG C 203 |
| Chain | Residue |
| C | TYR30 |
| C | TRP31 |
| C | PHE85 |
| C | GLN86 |
| C | ILE87 |
| C | HIS122 |
| C | TYR134 |
| C | HOH367 |
| C | HOH373 |
| C | HOH417 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MRD C 204 |
| Chain | Residue |
| C | LYS129 |
| C | TYR134 |
| C | MRD205 |
| C | HOH343 |
| E | HOH327 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue MRD C 205 |
| Chain | Residue |
| C | ILE87 |
| C | ILE88 |
| C | ILE89 |
| C | GLN94 |
| C | MRD204 |
| C | HOH397 |
| E | ASN170 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue MPD C 206 |
| Chain | Residue |
| C | LYS48 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for residue SPM D 201 |
| Chain | Residue |
| A | HIS49 |
| A | ILE50 |
| A | ASP52 |
| A | GLU55 |
| A | HOH314 |
| D | ASN22 |
| D | MET28 |
| D | GLU33 |
| D | GLU34 |
| D | TYR36 |
| D | GLU41 |
| D | HOH301 |
| D | HOH314 |
| D | HOH319 |
| D | HOH325 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue SP5 D 202 |
| Chain | Residue |
| D | TYR30 |
| D | TRP31 |
| D | GLU75 |
| D | PHE85 |
| D | GLN86 |
| D | ILE87 |
| D | HIS122 |
| D | TYR134 |
| D | HOH352 |
| D | HOH359 |
| D | HOH406 |
| D | HOH461 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue MRD D 203 |
| Chain | Residue |
| D | LYS129 |
| D | TYR134 |
| D | HOH308 |
| F | HOH227 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue MRD D 204 |
| Chain | Residue |
| D | TYR30 |
| D | ILE87 |
| D | ILE88 |
| D | ILE89 |
| D | GLN94 |
| D | HOH414 |
| F | ASN170 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue MPD D 205 |
| Chain | Residue |
| D | LYS48 |
| site_id | AE2 |
| Number of Residues | 11 |
| Details | binding site for residue SPM E 201 |
| Chain | Residue |
| A | TYR78 |
| D | HIS49 |
| D | ILE50 |
| D | ASP52 |
| D | GLU55 |
| D | HOH335 |
| E | GLU34 |
| E | GLU37 |
| E | GLU41 |
| E | HOH308 |
| E | HOH454 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951 |
| Chain | Residue | Details |
| A | TYR134 | |
| B | TYR134 | |
| C | TYR134 | |
| D | TYR134 | |
| E | TYR134 | |
| F | TYR134 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|Ref.3, ECO:0007744|PDB:4MJ8 |
| Chain | Residue | Details |
| A | MET28 | |
| E | GLU84 | |
| F | MET28 | |
| F | GLU84 | |
| A | GLU84 | |
| B | MET28 | |
| B | GLU84 | |
| C | MET28 | |
| C | GLU84 | |
| D | MET28 | |
| D | GLU84 | |
| E | MET28 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4 |
| Chain | Residue | Details |
| A | GLU33 | |
| B | GLU33 | |
| C | GLU33 | |
| D | GLU33 | |
| E | GLU33 | |
| F | GLU33 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4, ECO:0007744|PDB:4R87 |
| Chain | Residue | Details |
| A | GLU41 | |
| B | GLU41 | |
| C | GLU41 | |
| D | GLU41 | |
| E | GLU41 | |
| F | GLU41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R87 |
| Chain | Residue | Details |
| A | HIS49 | |
| B | HIS49 | |
| C | HIS49 | |
| D | HIS49 | |
| E | HIS49 | |
| F | HIS49 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|PubMed:26410587, ECO:0007744|PDB:5CNP |
| Chain | Residue | Details |
| A | GLU75 | |
| B | GLU75 | |
| C | GLU75 | |
| D | GLU75 | |
| E | GLU75 | |
| F | GLU75 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57, ECO:0007744|PDB:4R87 |
| Chain | Residue | Details |
| A | ILE87 | |
| E | GLN94 | |
| F | ILE87 | |
| F | GLN94 | |
| A | GLN94 | |
| B | ILE87 | |
| B | GLN94 | |
| C | ILE87 | |
| C | GLN94 | |
| D | ILE87 | |
| D | GLN94 | |
| E | ILE87 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57 |
| Chain | Residue | Details |
| A | ASN127 | |
| B | ASN127 | |
| C | ASN127 | |
| D | ASN127 | |
| E | ASN127 | |
| F | ASN127 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | SITE: Could be important for selectivity toward long polyamines => ECO:0000305|PubMed:25623305 |
| Chain | Residue | Details |
| A | GLU84 | |
| B | GLU84 | |
| C | GLU84 | |
| D | GLU84 | |
| E | GLU84 | |
| F | GLU84 |
