4HGR
Crystal structure of E56A/K67A mutant of 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphohydrolase from Bacteroides thetaiotaomicron
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 201 |
| Chain | Residue |
| A | ASP10 |
| A | ASP12 |
| A | ASP103 |
| A | HOH301 |
| A | HOH302 |
| A | HOH327 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 201 |
| Chain | Residue |
| B | HOH301 |
| B | HOH316 |
| B | HOH396 |
| B | ASP10 |
| B | ASP12 |
| B | ASP103 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 201 |
| Chain | Residue |
| C | ASP10 |
| C | ASP12 |
| C | ASP103 |
| C | HOH302 |
| C | HOH303 |
| C | HOH369 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 201 |
| Chain | Residue |
| D | ASP10 |
| D | ASP12 |
| D | ASP103 |
| D | HOH308 |
| D | HOH312 |
| D | HOH398 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 201 |
| Chain | Residue |
| E | ASP10 |
| E | ASP12 |
| E | ASP103 |
| E | HOH301 |
| E | HOH316 |
| E | HOH342 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 201 |
| Chain | Residue |
| F | ASP10 |
| F | ASP12 |
| F | ASP103 |
| F | HOH301 |
| F | HOH302 |
| F | HOH352 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 201 |
| Chain | Residue |
| G | ASP10 |
| G | ASP12 |
| G | ASP103 |
| G | HOH302 |
| G | HOH303 |
| G | HOH320 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 201 |
| Chain | Residue |
| H | ASP10 |
| H | ASP12 |
| H | ASP103 |
| H | HOH315 |
| H | HOH322 |
| H | HOH324 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18986982, ECO:0000269|PubMed:23848398, ECO:0007744|PDB:3E84, ECO:0007744|PDB:4HGO, ECO:0007744|PDB:4HGQ, ECO:0007744|PDB:4HGR |
| Chain | Residue | Details |
| A | ASP10 | |
| D | ASP10 | |
| D | ASP12 | |
| D | ASP103 | |
| E | ASP10 | |
| E | ASP12 | |
| E | ASP103 | |
| F | ASP10 | |
| F | ASP12 | |
| F | ASP103 | |
| G | ASP10 | |
| A | ASP12 | |
| G | ASP12 | |
| G | ASP103 | |
| H | ASP10 | |
| H | ASP12 | |
| H | ASP103 | |
| A | ASP103 | |
| B | ASP10 | |
| B | ASP12 | |
| B | ASP103 | |
| C | ASP10 | |
| C | ASP12 | |
| C | ASP103 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18986982, ECO:0000305|PubMed:23848398, ECO:0007744|PDB:3E81, ECO:0007744|PDB:3E8M, ECO:0007744|PDB:4HGO |
| Chain | Residue | Details |
| A | THR34 | |
| E | ARG64 | |
| F | THR34 | |
| F | ARG64 | |
| G | THR34 | |
| G | ARG64 | |
| H | THR34 | |
| H | ARG64 | |
| A | ARG64 | |
| B | THR34 | |
| B | ARG64 | |
| C | THR34 | |
| C | ARG64 | |
| D | THR34 | |
| D | ARG64 | |
| E | THR34 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18986982, ECO:0000305|PubMed:23848398, ECO:0007744|PDB:3E81, ECO:0007744|PDB:3E84, ECO:0007744|PDB:4HGO |
| Chain | Residue | Details |
| A | THR54 | |
| E | LYS80 | |
| F | THR54 | |
| F | LYS80 | |
| G | THR54 | |
| G | LYS80 | |
| H | THR54 | |
| H | LYS80 | |
| A | LYS80 | |
| B | THR54 | |
| B | LYS80 | |
| C | THR54 | |
| C | LYS80 | |
| D | THR54 | |
| D | LYS80 | |
| E | THR54 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18986982, ECO:0007744|PDB:3E81, ECO:0007744|PDB:3E84 |
| Chain | Residue | Details |
| A | ASN106 | |
| B | ASN106 | |
| C | ASN106 | |
| D | ASN106 | |
| E | ASN106 | |
| F | ASN106 | |
| G | ASN106 | |
| H | ASN106 |
