3E84
Structure-function Analysis of 2-Keto-3-deoxy-D-glycero-D-galacto-nononate-9-phosphate (KDN) Phosphatase Defines a New Clad Within the Type C0 HAD Subfamily
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 701 |
| Chain | Residue |
| A | ASP10 |
| A | ASP12 |
| A | ASP103 |
| A | WO4801 |
| B | HOH882 |
| B | HOH1001 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 702 |
| Chain | Residue |
| B | WO4802 |
| B | HOH832 |
| B | HOH1143 |
| B | ASP10 |
| B | ASP12 |
| B | ASP103 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 703 |
| Chain | Residue |
| B | HOH935 |
| B | HOH936 |
| C | ASP10 |
| C | ASP12 |
| C | ASP103 |
| C | WO4803 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 704 |
| Chain | Residue |
| B | HOH1086 |
| B | HOH1093 |
| D | ASP10 |
| D | ASP12 |
| D | ASP103 |
| D | WO4804 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE WO4 A 801 |
| Chain | Residue |
| A | ASP10 |
| A | ILE11 |
| A | ASP12 |
| A | THR54 |
| A | GLY55 |
| A | GLU56 |
| A | LYS80 |
| A | ASN106 |
| A | MG701 |
| B | HOH857 |
| B | HOH882 |
| B | HOH1001 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE WO4 B 802 |
| Chain | Residue |
| B | ASP10 |
| B | ILE11 |
| B | ASP12 |
| B | THR54 |
| B | GLY55 |
| B | GLU56 |
| B | LYS80 |
| B | ASN106 |
| B | MG702 |
| B | HOH832 |
| B | HOH900 |
| B | HOH1143 |
| B | HOH1248 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE WO4 C 803 |
| Chain | Residue |
| B | HOH935 |
| B | HOH936 |
| B | HOH1215 |
| C | ASP10 |
| C | ILE11 |
| C | ASP12 |
| C | THR54 |
| C | GLY55 |
| C | GLU56 |
| C | LYS80 |
| C | ASN106 |
| C | MG703 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE WO4 D 804 |
| Chain | Residue |
| B | HOH1086 |
| B | HOH1093 |
| D | ASP10 |
| D | ILE11 |
| D | ASP12 |
| D | THR54 |
| D | GLY55 |
| D | GLU56 |
| D | LYS80 |
| D | ASN106 |
| D | MG704 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 802 |
| Chain | Residue |
| A | HIS44 |
| A | GLY47 |
| A | ASP71 |
| B | HOH1296 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 803 |
| Chain | Residue |
| B | HIS44 |
| B | ASP71 |
| B | HOH1054 |
| B | HOH1276 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 803 |
| Chain | Residue |
| A | PHE74 |
| A | ALA83 |
| A | GLU86 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 804 |
| Chain | Residue |
| C | HIS44 |
| C | ASP71 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 804 |
| Chain | Residue |
| A | PRO124 |
| A | PHE125 |
| A | ARG128 |
| B | PHE134 |
| B | HOH1150 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| 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 | |
| A | ASP12 | |
| A | ASP103 | |
| B | ASP10 | |
| B | ASP12 | |
| B | ASP103 | |
| C | ASP10 | |
| C | ASP12 | |
| C | ASP103 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| 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 | |
| A | ARG64 | |
| B | THR34 | |
| B | ARG64 | |
| C | THR34 | |
| C | ARG64 | |
| D | THR34 | |
| D | ARG64 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | |
| A | LYS80 | |
| B | THR54 | |
| B | LYS80 | |
| C | THR54 | |
| C | LYS80 | |
| D | THR54 | |
| D | LYS80 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 |
