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 | 10 |
Details | BINDING: in other chain => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O61 |
Chain | Residue | Details |
A | TYR17 | |
B | LYS176 | |
A | ARG67 | |
A | GLU127 | |
A | ASP150 | |
A | LYS176 | |
B | TYR17 | |
B | ARG67 | |
B | GLU127 | |
B | ASP150 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O61 |
Chain | Residue | Details |
A | LYS38 | |
B | LYS38 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O6Z |
Chain | Residue | Details |
A | ALA85 | |
A | ALA100 | |
A | GLU104 | |
A | GLU151 | |
B | ALA85 | |
B | ALA100 | |
B | GLU104 | |
B | GLU151 |