6D72
Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Yersinia pestis in complex with calcium ions.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004145 | molecular_function | diamine N-acetyltransferase activity |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0046872 | molecular_function | metal ion binding |
B | 0004145 | molecular_function | diamine N-acetyltransferase activity |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0046872 | molecular_function | metal ion binding |
C | 0004145 | molecular_function | diamine N-acetyltransferase activity |
C | 0016746 | molecular_function | acyltransferase activity |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 201 |
Chain | Residue |
A | GLU35 |
A | GLU76 |
A | CA202 |
A | HOH321 |
B | GLU35 |
B | HOH343 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 202 |
Chain | Residue |
B | GLU76 |
B | HOH314 |
B | HOH351 |
A | GLU35 |
A | CA201 |
B | GLU35 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue PEG A 203 |
Chain | Residue |
A | TYR32 |
A | PHE34 |
A | GLU35 |
A | GLU57 |
A | HOH333 |
B | ASN78 |
B | HOH351 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MLI A 204 |
Chain | Residue |
A | GLU76 |
A | ILE123 |
A | GLU149 |
A | PHE150 |
B | TYR121 |
B | MLI202 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue PEG B 201 |
Chain | Residue |
A | GLU15 |
B | PRO18 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MLI B 202 |
Chain | Residue |
A | MLI204 |
B | GLU76 |
B | GLU149 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue CA C 201 |
Chain | Residue |
C | GLU35 |
C | GLU35 |
C | GLU76 |
C | HOH339 |
C | HOH346 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MLI C 204 |
Chain | Residue |
C | ARG31 |
C | TYR32 |
C | TYR38 |
C | LEU71 |
C | GLU73 |
C | ILE89 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue MLI C 205 |
Chain | Residue |
B | GLU15 |
C | HIS21 |
C | ASN25 |
C | PHE41 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue MLI C 206 |
Chain | Residue |
C | ILE152 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residues MLI C 202 and MLI C 203 |
Chain | Residue |
C | GLU76 |
C | ARG83 |
C | ILE123 |
C | GLU149 |
C | GLU149 |
C | HOH301 |
C | HOH304 |
C | HOH314 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residues MLI C 202 and MLI C 203 |
Chain | Residue |
C | GLU76 |
C | ARG83 |
C | ILE123 |
C | GLU149 |
C | GLU149 |
C | HOH301 |
C | HOH304 |
C | HOH314 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residues MLI C 202 and MLI C 203 |
Chain | Residue |
C | GLU76 |
C | ARG83 |
C | ILE123 |
C | GLU149 |
C | GLU149 |
C | HOH301 |
C | HOH304 |
C | HOH314 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residues MLI C 202 and MLI C 203 |
Chain | Residue |
C | GLU76 |
C | ARG83 |
C | ILE123 |
C | GLU149 |
C | GLU149 |
C | HOH301 |
C | HOH304 |
C | HOH314 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residues MLI C 202 and MLI C 203 |
Chain | Residue |
C | GLU76 |
C | ARG83 |
C | ILE123 |
C | GLU149 |
C | GLU149 |
C | HOH301 |
C | HOH304 |
C | HOH314 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residues MLI C 202 and MLI C 203 |
Chain | Residue |
C | GLU76 |
C | ARG83 |
C | ILE123 |
C | GLU149 |
C | GLU149 |
C | HOH301 |
C | HOH304 |
C | HOH314 |