2XCU
Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
A | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
A | 0009245 | biological_process | lipid A biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0043842 | molecular_function | Kdo transferase activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
B | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
B | 0009245 | biological_process | lipid A biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0043842 | molecular_function | Kdo transferase activity |
C | 0005886 | cellular_component | plasma membrane |
C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
C | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
C | 0009245 | biological_process | lipid A biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0043842 | molecular_function | Kdo transferase activity |
D | 0005886 | cellular_component | plasma membrane |
D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
D | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
D | 0009245 | biological_process | lipid A biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0043842 | molecular_function | Kdo transferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE C5P A 400 |
Chain | Residue |
A | SER182 |
A | ASN273 |
A | GLU276 |
A | HOH2033 |
A | HOH2034 |
A | VAL210 |
A | PRO211 |
A | ARG212 |
A | PHE247 |
A | GLY248 |
A | ILE249 |
A | LEU250 |
A | HIS272 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE A 1353 |
Chain | Residue |
A | PHE3 |
A | VAL5 |
A | ARG8 |
A | PHE53 |
A | PRO55 |
A | CIT1356 |
C | ARG99 |
C | GLU100 |
C | PHE101 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE A 1354 |
Chain | Residue |
A | ARG99 |
A | GLU100 |
A | PHE101 |
C | PHE3 |
C | VAL5 |
C | ARG8 |
C | PHE53 |
C | PRO55 |
C | CIT1353 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIT A 1355 |
Chain | Residue |
A | ILE183 |
A | HIS184 |
A | THR185 |
A | ARG212 |
A | HIS213 |
A | ASN216 |
A | PHE220 |
C | HIS184 |
C | THR185 |
C | HIS213 |
C | ASN216 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT A 1356 |
Chain | Residue |
A | GLN2 |
A | PHE3 |
A | GLU4 |
A | VAL5 |
A | LEU6 |
A | 1PE1353 |
C | ARG99 |
C | LYS121 |
C | SER123 |
C | ILE125 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE C5P B 400 |
Chain | Residue |
B | SER182 |
B | VAL210 |
B | PRO211 |
B | ARG212 |
B | PHE247 |
B | GLY248 |
B | ILE249 |
B | LEU250 |
B | LYS251 |
B | HIS272 |
B | ASN273 |
B | GLU276 |
B | HOH2020 |
B | HOH2028 |
B | HOH2029 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1PE B 1353 |
Chain | Residue |
B | ARG99 |
B | GLU100 |
B | PHE101 |
B | TRP102 |
D | PHE3 |
D | VAL5 |
D | ARG8 |
D | PHE53 |
D | PRO55 |
D | CIT1354 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CIT B 1354 |
Chain | Residue |
B | GLN2 |
B | PHE3 |
B | GLU4 |
B | VAL5 |
B | LEU6 |
D | ARG99 |
D | LYS121 |
D | SER123 |
D | 1PE1353 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME B 1355 |
Chain | Residue |
B | PHE9 |
B | ARG84 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE C5P C 400 |
Chain | Residue |
C | ASN273 |
C | GLU276 |
C | HOH2025 |
C | HOH2026 |
C | HOH2027 |
C | SER182 |
C | VAL210 |
C | PRO211 |
C | ARG212 |
C | ILE214 |
C | PHE247 |
C | GLY248 |
C | ILE249 |
C | LEU250 |
C | LYS251 |
C | HIS272 |
site_id | BC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIT C 1353 |
Chain | Residue |
A | ARG99 |
A | LYS121 |
A | SER123 |
A | ILE125 |
A | 1PE1354 |
A | HOH2017 |
C | GLN2 |
C | PHE3 |
C | GLU4 |
C | VAL5 |
C | LEU6 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME C 1354 |
Chain | Residue |
C | PHE9 |
C | PHE80 |
site_id | BC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE C5P D 400 |
Chain | Residue |
D | SER182 |
D | VAL210 |
D | PRO211 |
D | ARG212 |
D | PHE247 |
D | GLY248 |
D | ILE249 |
D | LEU250 |
D | LYS251 |
D | HIS272 |
D | ASN273 |
D | GLU276 |
D | HOH2024 |
D | HOH2025 |
D | HOH2026 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1PE D 1353 |
Chain | Residue |
B | PHE3 |
B | VAL5 |
B | ARG8 |
B | PHE53 |
B | PRO55 |
B | CIT1354 |
D | ARG99 |
D | GLU100 |
D | PHE101 |
D | TRP102 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CIT D 1354 |
Chain | Residue |
B | LYS121 |
B | SER123 |
B | ILE125 |
B | 1PE1353 |
D | GLN2 |
D | PHE3 |
D | GLU4 |
D | VAL5 |
D | LEU6 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME D 1355 |
Chain | Residue |
D | PHE10 |
D | PHE80 |
D | ARG84 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22474366 |
Chain | Residue | Details |
A | GLU31 | |
B | GLU31 | |
C | GLU31 | |
D | GLU31 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22474366, ECO:0007744|PDB:2XCU |
Chain | Residue | Details |
A | PRO211 | |
D | PRO211 | |
D | PHE247 | |
D | ASN273 | |
A | PHE247 | |
A | ASN273 | |
B | PRO211 | |
B | PHE247 | |
B | ASN273 | |
C | PRO211 | |
C | PHE247 | |
C | ASN273 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | GLU98 | |
A | LYS162 | |
B | GLU98 | |
B | LYS162 | |
C | GLU98 | |
C | LYS162 | |
D | GLU98 | |
D | LYS162 |