5KGN
1.95A resolution structure of independent phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (2d)
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 | 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 | 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 | 3 |
| Details | binding site for residue CL A 601 |
| Chain | Residue |
| A | ARG97 |
| A | ASN336 |
| A | HOH869 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | ARG287 |
| A | HIS147 |
| A | ARG177 |
| A | ASP178 |
| A | ARG210 |
| A | ARG216 |
| A | ARG284 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | ILE50 |
| A | LEU51 |
| A | ALA53 |
| A | THR55 |
| A | HOH808 |
| A | HOH944 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 604 |
| Chain | Residue |
| A | ASP426 |
| A | HIS430 |
| A | HIS485 |
| A | HOH770 |
| A | HOH998 |
| A | HOH1000 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 605 |
| Chain | Residue |
| A | ASP37 |
| A | SER86 |
| A | ASP467 |
| A | HIS468 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 601 |
| Chain | Residue |
| B | ARG97 |
| B | ASN336 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | HIS147 |
| B | ARG177 |
| B | ASP178 |
| B | ARG210 |
| B | ARG216 |
| B | ARG284 |
| B | ARG287 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 603 |
| Chain | Residue |
| B | ILE50 |
| B | LEU51 |
| B | ALA53 |
| B | THR55 |
| B | HOH735 |
| B | HOH807 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 604 |
| Chain | Residue |
| B | ASP426 |
| B | HIS430 |
| B | HIS485 |
| B | HOH711 |
| B | HOH933 |
| B | HOH952 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 605 |
| Chain | Residue |
| B | ASP37 |
| B | SER86 |
| B | ASP467 |
| B | HIS468 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide ACE C 0 and DTY C 1 |
| Chain | Residue |
| A | GLU87 |
| A | PHE365 |
| A | PHE366 |
| C | ASP2 |
| C | TYR3 |
| C | ASP6 |
| C | TYR7 |
| C | CYS8 |
| C | TYR9 |
| C | TYR11 |
| C | NH212 |
| C | HOH104 |
| C | HOH107 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide ACE C 0 and CYS C 8 |
| Chain | Residue |
| C | DTY1 |
| C | ASP2 |
| C | ASP6 |
| C | TYR7 |
| C | TYR9 |
| C | LEU10 |
| C | TYR11 |
| C | NH212 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide DTY C 1 and ASP C 2 |
| Chain | Residue |
| A | GLU87 |
| A | ARG289 |
| A | PHE365 |
| A | PHE366 |
| C | ACE0 |
| C | TYR3 |
| C | ASP6 |
| C | CYS8 |
| C | TYR9 |
| C | TYR11 |
| C | NH212 |
| C | HOH101 |
| C | HOH104 |
| C | HOH106 |
| C | HOH107 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide TYR C 11 and NH2 C 12 |
| Chain | Residue |
| A | ASN85 |
| A | GLU87 |
| C | DTY1 |
| C | CYS8 |
| C | TYR9 |
| C | LEU10 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide ACE D 0 and CYS D 8 |
| Chain | Residue |
| D | TYR11 |
| D | NH212 |
| D | DTY1 |
| D | ASP2 |
| D | ASP6 |
| D | TYR7 |
| D | TYR9 |
| D | LEU10 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide ACE D 0 and DTY D 1 |
| Chain | Residue |
| B | GLU87 |
| B | PHE365 |
| B | PHE366 |
| D | ASP2 |
| D | TYR3 |
| D | ASP6 |
| D | TYR7 |
| D | CYS8 |
| D | TYR9 |
| D | NH212 |
| D | HOH103 |
| D | HOH105 |
| site_id | AD8 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide DTY D 1 and ASP D 2 |
| Chain | Residue |
| B | GLU87 |
| B | ARG289 |
| B | PHE365 |
| B | PHE366 |
| D | ACE0 |
| D | TYR3 |
| D | ASP6 |
| D | CYS8 |
| D | TYR9 |
| D | NH212 |
| D | HOH101 |
| D | HOH103 |
| D | HOH105 |
| D | HOH106 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide TYR D 11 and NH2 D 12 |
| Chain | Residue |
| B | ASN85 |
| B | GLU87 |
| B | HOH727 |
| D | DTY1 |
| D | CYS8 |
| D | TYR9 |
| D | LEU10 |
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 |
