5KGM
2.95A resolution structure of Apo independent phosphoglycerate mutase from C. elegans (monoclinic form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006007 | biological_process | glucose catabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006007 | biological_process | glucose catabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| 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 | 2 |
| Details | binding site for residue CL A 601 |
| Chain | Residue |
| A | ARG97 |
| A | ASN336 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 602 |
| Chain | Residue |
| A | ARG216 |
| A | ARG284 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue MN A 603 |
| Chain | Residue |
| A | ASP426 |
| A | HIS430 |
| A | HIS485 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 604 |
| Chain | Residue |
| A | LYS359 |
| A | ASP467 |
| A | HIS468 |
| A | ASP37 |
| A | SER86 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 601 |
| Chain | Residue |
| B | ARG97 |
| B | ASN336 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 602 |
| Chain | Residue |
| B | ARG216 |
| B | ARG284 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue MN B 603 |
| Chain | Residue |
| B | ASP426 |
| B | HIS430 |
| B | HIS485 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 604 |
| Chain | Residue |
| B | ASP37 |
| B | SER86 |
| B | LYS359 |
| B | ASP467 |
| B | HIS468 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q9X519 |
| Chain | Residue | Details |
| A | SER86 | |
| B | SER86 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9X519 |
| Chain | Residue | Details |
| A | ASP37 | |
| A | HIS430 | |
| A | ASP467 | |
| A | HIS468 | |
| A | HIS485 | |
| B | ASP37 | |
| B | SER86 | |
| B | HIS147 | |
| B | ARG177 | |
| B | ARG210 | |
| B | ARG216 | |
| A | SER86 | |
| B | ARG284 | |
| B | LYS359 | |
| B | ASP426 | |
| B | HIS430 | |
| B | ASP467 | |
| B | HIS468 | |
| B | HIS485 | |
| A | HIS147 | |
| A | ARG177 | |
| A | ARG210 | |
| A | ARG216 | |
| A | ARG284 | |
| A | LYS359 | |
| A | ASP426 |
