1RO7
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CSF C 1001 |
| Chain | Residue |
| A | GLY8 |
| A | THR131 |
| A | SER132 |
| A | GLY133 |
| A | GLY152 |
| A | ILE153 |
| A | ASP154 |
| A | PHE155 |
| A | TYR156 |
| A | GLY159 |
| A | SER161 |
| A | ASN9 |
| A | TYR162 |
| A | PHE178 |
| A | TYR185 |
| A | HIS188 |
| A | HOH262 |
| A | HOH313 |
| A | HOH326 |
| C | HOH4007 |
| C | HOH4050 |
| C | HOH4081 |
| A | GLY10 |
| A | CYS30 |
| A | ASN31 |
| A | GLN32 |
| A | ASN51 |
| A | LEU54 |
| A | GLN58 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CSF C 2001 |
| Chain | Residue |
| B | GLY8 |
| B | ASN9 |
| B | GLY10 |
| B | CYS30 |
| B | ASN31 |
| B | GLN32 |
| B | ASN51 |
| B | LEU54 |
| B | GLN58 |
| B | THR131 |
| B | SER132 |
| B | GLY133 |
| B | GLY152 |
| B | ILE153 |
| B | ASP154 |
| B | PHE155 |
| B | PHE178 |
| B | HIS188 |
| B | HOH436 |
| C | HOH4005 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CSF C 3001 |
| Chain | Residue |
| C | GLY8 |
| C | ASN9 |
| C | GLY10 |
| C | CYS30 |
| C | ASN31 |
| C | GLN32 |
| C | ASN51 |
| C | LEU54 |
| C | GLN58 |
| C | THR131 |
| C | SER132 |
| C | GLY133 |
| C | GLY152 |
| C | ILE153 |
| C | ASP154 |
| C | PHE155 |
| C | TYR156 |
| C | SER161 |
| C | TYR162 |
| C | HIS188 |
| C | HOH4014 |
| C | HOH4027 |
| C | HOH4082 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CSF C 4001 |
| Chain | Residue |
| D | GLY8 |
| D | ASN9 |
| D | GLY10 |
| D | ASN31 |
| D | GLN32 |
| D | ASN51 |
| D | LEU54 |
| D | THR131 |
| D | SER132 |
| D | GLY152 |
| D | ILE153 |
| D | ASP154 |
| D | PHE155 |
| D | TYR156 |
| D | HIS188 |
| D | HOH272 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 14730352 |
| Chain | Residue | Details |
| A | TYR156 | |
| A | ARG129 | |
| A | TYR162 | |
| A | HIS188 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 14730352 |
| Chain | Residue | Details |
| B | ARG129 | |
| B | HIS188 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 14730352 |
| Chain | Residue | Details |
| C | TYR156 | |
| C | ARG129 | |
| C | TYR162 | |
| C | HIS188 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 14730352 |
| Chain | Residue | Details |
| D | TYR156 | |
| D | ARG129 | |
| D | HIS188 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 840 |
| Chain | Residue | Details |
| A | CYS137 | electrostatic stabiliser |
| A | GLN168 | electrostatic stabiliser |
| A | LEU174 | electrostatic stabiliser |
| A | LEU200 | activator, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 840 |
| Chain | Residue | Details |
| B | CYS137 | electrostatic stabiliser |
| B | GLN168 | electrostatic stabiliser |
| B | LEU174 | electrostatic stabiliser |
| B | LEU200 | activator, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 840 |
| Chain | Residue | Details |
| C | CYS137 | electrostatic stabiliser |
| C | GLN168 | electrostatic stabiliser |
| C | LEU174 | electrostatic stabiliser |
| C | LEU200 | activator, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 840 |
| Chain | Residue | Details |
| D | CYS137 | electrostatic stabiliser |
| D | GLN168 | electrostatic stabiliser |
| D | LEU174 | electrostatic stabiliser |
| D | LEU200 | activator, proton acceptor, proton donor |
