2ZKT
Structure of PH0037 protein from Pyrococcus horikoshii
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004619 | molecular_function | phosphoglycerate mutase activity |
A | 0006096 | biological_process | glycolytic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0046537 | molecular_function | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004619 | molecular_function | phosphoglycerate mutase activity |
B | 0006096 | biological_process | glycolytic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0046537 | molecular_function | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 413 |
Chain | Residue |
A | GLU42 |
A | THR372 |
A | ASP373 |
A | HOH484 |
A | HOH485 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 414 |
Chain | Residue |
A | ASP13 |
A | SER60 |
A | ASP346 |
A | HIS347 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 415 |
Chain | Residue |
A | ASP305 |
A | HIS309 |
A | HIS356 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 413 |
Chain | Residue |
B | GLU42 |
B | THR372 |
B | ASP373 |
B | HOH501 |
B | HOH502 |
B | HOH524 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 414 |
Chain | Residue |
B | ASP13 |
B | SER60 |
B | ASP346 |
B | HIS347 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 415 |
Chain | Residue |
B | ASP305 |
B | HIS309 |
B | HIS356 |