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 | 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 | 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 | 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 | MSE28 | |
A | GLU84 | |
B | MSE28 | |
B | GLU84 | |
C | MSE28 | |
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 |