2WLF
Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0008374 | molecular_function | O-acyltransferase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0050208 | molecular_function | polysialic-acid O-acetyltransferase activity |
A | 0070207 | biological_process | protein homotrimerization |
B | 0005829 | cellular_component | cytosol |
B | 0008374 | molecular_function | O-acyltransferase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0050208 | molecular_function | polysialic-acid O-acetyltransferase activity |
B | 0070207 | biological_process | protein homotrimerization |
C | 0005829 | cellular_component | cytosol |
C | 0008374 | molecular_function | O-acyltransferase activity |
C | 0016740 | molecular_function | transferase activity |
C | 0050208 | molecular_function | polysialic-acid O-acetyltransferase activity |
C | 0070207 | biological_process | protein homotrimerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 1215 |
Chain | Residue |
A | ARG197 |
A | LYS198 |
A | MET199 |
A | TYR200 |
A | HOH2110 |
B | MET120 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 1216 |
Chain | Residue |
A | SER36 |
A | PHE60 |
A | GLN81 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1217 |
Chain | Residue |
A | ASN16 |
A | ALA62 |
A | ASP63 |
A | ALA84 |
A | HOH2021 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 1218 |
Chain | Residue |
A | MET5 |
A | HOH2112 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1219 |
Chain | Residue |
A | LYS154 |
A | GLY155 |
A | TYR171 |
A | SER173 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 1220 |
Chain | Residue |
A | ASN34 |
A | ASN35 |
A | SER36 |
A | ASN56 |
A | ILE57 |
A | THR58 |
A | GLN81 |
A | LYS100 |
site_id | AC7 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ACO A 1221 |
Chain | Residue |
A | ARG116 |
A | ASP119 |
A | HIS121 |
A | ILE123 |
A | ASN133 |
A | LEU153 |
A | LYS154 |
A | TYR171 |
A | LYS172 |
A | HOH2113 |
A | HOH2114 |
A | HOH2115 |
A | HOH2116 |
A | HOH2117 |
C | ALA110 |
C | TRP145 |
C | GLY147 |
C | ARG148 |
C | VAL163 |
C | GLY165 |
C | SER166 |
C | VAL180 |
C | GLY183 |
C | VAL189 |
C | LYS190 |
C | ASN192 |
C | HOH2047 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1216 |
Chain | Residue |
A | MET199 |
A | HOH2107 |
B | ALA96 |
B | GLU97 |
B | HOH2055 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 1217 |
Chain | Residue |
B | ASN90 |
B | GLY91 |
B | GLY112 |
B | TYR113 |
site_id | BC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ACO B 1218 |
Chain | Residue |
A | MET108 |
A | TRP145 |
A | GLY147 |
A | ARG148 |
A | VAL163 |
A | GLY165 |
A | SER166 |
A | VAL180 |
A | GLY183 |
A | VAL189 |
B | ARG116 |
B | ASP119 |
B | HIS121 |
B | ILE123 |
B | ASN133 |
B | LYS154 |
B | TYR171 |
B | LYS172 |
B | LYS175 |
B | HOH2037 |
B | HOH2056 |
B | HOH2058 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT C 1216 |
Chain | Residue |
C | ALA110 |
C | HIS111 |
C | ARG148 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 1217 |
Chain | Residue |
A | MET120 |
C | ARG197 |
C | LYS198 |
C | MET199 |
C | TYR200 |
site_id | BC4 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ACO C 1218 |
Chain | Residue |
B | VAL163 |
B | GLY165 |
B | SER166 |
B | GLY183 |
B | VAL189 |
B | LYS190 |
C | ARG116 |
C | ASP119 |
C | HIS121 |
C | ILE123 |
C | ASN133 |
C | LYS154 |
C | TYR171 |
C | HOH2029 |
C | HOH2036 |
C | HOH2071 |
C | HOH2072 |
C | HOH2073 |
C | HOH2075 |
C | HOH2076 |
C | HOH2077 |
B | MET108 |
B | ALA110 |
B | TRP145 |
B | GLY147 |
B | ARG148 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19525232 |
Chain | Residue | Details |
A | ASP119 | |
B | SER166 | |
B | TYR171 | |
B | LYS190 | |
C | ASP119 | |
C | ARG148 | |
C | LYS154 | |
C | SER166 | |
C | TYR171 | |
C | LYS190 | |
A | ARG148 | |
A | LYS154 | |
A | SER166 | |
A | TYR171 | |
A | LYS190 | |
B | ASP119 | |
B | ARG148 | |
B | LYS154 |