3O69
Structure of the E100A E.coli GDP-mannose hydrolase (yffh) in complex with Mg++
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006753 | biological_process | nucleoside phosphate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| A | 0019693 | biological_process | ribose phosphate metabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052751 | molecular_function | GDP-mannose hydrolase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006753 | biological_process | nucleoside phosphate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| B | 0019693 | biological_process | ribose phosphate metabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052751 | molecular_function | GDP-mannose hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 202 |
| Chain | Residue |
| A | ALA85 |
| A | GLU104 |
| A | HOH213 |
| A | HOH297 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 6073 |
| Chain | Residue |
| A | ASP15 |
| A | ASN16 |
| B | HIS188 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 210 |
| Chain | Residue |
| A | GLU40 |
| B | ARG44 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 214 |
| Chain | Residue |
| A | TRP71 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 219 |
| Chain | Residue |
| A | THR2 |
| B | GLN65 |
| B | PHE66 |
| B | ASP152 |
| B | HOH413 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 215 |
| Chain | Residue |
| B | ARG44 |
| B | HOH252 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 203 |
| Chain | Residue |
| B | HOH236 |
| B | HOH305 |
| B | HOH307 |
| B | HOH308 |
| B | HOH405 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 202 |
| Chain | Residue |
| B | ALA85 |
| B | GLU104 |
| B | HOH199 |
| B | HOH218 |
| B | HOH315 |
| B | HOH365 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 250 |
| Chain | Residue |
| B | HOH230 |
| B | HOH316 |
| B | HOH317 |
| B | HOH318 |
| B | HOH319 |
| B | HOH345 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 210 |
| Chain | Residue |
| B | TRP71 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 192 |
| Chain | Residue |
| B | GLU92 |
| B | PRO93 |
| B | GLU94 |
| B | LYS114 |
| B | PHE132 |
| B | HOH302 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 13 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"21638333","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O61","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21638333","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O61","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21638333","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O6Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 137 |
| Details | Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 27 |
| Details | Motif: {"description":"Nudix box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
