1X9H
Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
A | 0004476 | molecular_function | mannose-6-phosphate isomerase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0097367 | molecular_function | carbohydrate derivative binding |
A | 1901135 | biological_process | carbohydrate derivative metabolic process |
B | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
B | 0004476 | molecular_function | mannose-6-phosphate isomerase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0097367 | molecular_function | carbohydrate derivative binding |
B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 501 |
Chain | Residue |
B | ARG104 |
B | ARG105 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | ARG299 |
A | ARG300 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | ARG104 |
A | ARG105 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | HOH846 |
B | ARG79 |
A | GLN179 |
A | ARG181 |
A | ARG284 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 505 |
Chain | Residue |
B | GLN179 |
B | ARG181 |
B | ARG284 |
B | HOH780 |
B | HOH878 |
B | HOH894 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE F6R B 700 |
Chain | Residue |
A | HIS219 |
B | MET45 |
B | GLY46 |
B | GLY47 |
B | SER48 |
B | SER87 |
B | TYR88 |
B | SER89 |
B | THR92 |
B | PRO134 |
B | ARG135 |
B | GLU203 |
B | LYS298 |
B | HOH723 |
B | HOH887 |
B | HOH888 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE F6R A 701 |
Chain | Residue |
A | MET45 |
A | GLY46 |
A | GLY47 |
A | SER48 |
A | SER87 |
A | TYR88 |
A | SER89 |
A | THR92 |
A | PRO134 |
A | ARG135 |
A | GLU203 |
A | LYS298 |
A | HOH723 |
A | HOH760 |
B | HIS219 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | ASP53 |
A | LYS72 |
A | ARG191 |
A | TYR195 |
A | HOH739 |
A | HOH757 |
A | HOH784 |
A | HOH909 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 602 |
Chain | Residue |
A | THR233 |
A | GLN242 |
A | HOH893 |
A | HOH898 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 603 |
Chain | Residue |
A | SER89 |
A | ASN91 |
A | THR92 |
A | ILE93 |
A | LYS298 |
A | HOH720 |
A | HOH751 |
A | HOH814 |
B | ARG117 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 605 |
Chain | Residue |
B | VAL27 |
B | GLU28 |
B | GLU30 |
B | LYS103 |
B | ARG104 |
B | ARG106 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305 |
Chain | Residue | Details |
A | GLU203 | |
A | LYS298 | |
B | GLU203 | |
B | LYS298 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305 |
Chain | Residue | Details |
A | HIS219 | |
B | HIS219 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | SER48 | |
A | SER87 | |
A | THR92 | |
B | SER48 | |
B | SER87 | |
B | THR92 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 15518558 |
Chain | Residue | Details |
A | ARG135 | |
A | LYS298 | |
A | HIS219 | |
A | GLU203 |
site_id | CSA2 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 15518558 |
Chain | Residue | Details |
B | ARG135 | |
B | LYS298 | |
B | HIS219 | |
B | GLU203 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 736 |
Chain | Residue | Details |
A | ARG135 | electrostatic stabiliser |
A | GLU203 | proton acceptor, proton donor |
A | HIS219 | proton acceptor, proton donor |
A | LYS298 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 736 |
Chain | Residue | Details |
B | ARG135 | electrostatic stabiliser |
B | GLU203 | proton acceptor, proton donor |
B | HIS219 | proton acceptor, proton donor |
B | LYS298 | proton acceptor, proton donor |