3O6Z
Structure of the D152A 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 | 5 |
Details | BINDING SITE FOR RESIDUE MG A 202 |
Chain | Residue |
A | ALA85 |
A | GLU104 |
A | HOH311 |
A | HOH324 |
A | HOH417 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 201 |
Chain | Residue |
B | HOH229 |
B | HOH414 |
B | HOH415 |
B | GLU100 |
B | GLU104 |
B | GLU151 |
B | MG202 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MG B 202 |
Chain | Residue |
B | ALA85 |
B | GLU104 |
B | GLU151 |
B | MG201 |
B | HOH214 |
B | HOH240 |
B | HOH347 |
B | HOH414 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 204 |
Chain | Residue |
B | ARG113 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 203 |
Chain | Residue |
B | GLN4 |
B | THR28 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG B 205 |
Chain | Residue |
B | GLU94 |
B | VAL95 |
B | LYS99 |
B | HOH327 |
B | HOH350 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TRS B 206 |
Chain | Residue |
B | ARG64 |
B | ILE81 |
B | MET166 |
B | GLU171 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG B 192 |
Chain | Residue |
A | ILE8 |
A | ARG36 |
B | ASP15 |
B | THR19 |
B | HIS21 |
B | ASP43 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
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 |