3ZLG
Structure of group A Streptococcal enolase K362A mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006096 | biological_process | glycolytic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0009986 | cellular_component | cell surface |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006096 | biological_process | glycolytic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0009986 | cellular_component | cell surface |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006096 | biological_process | glycolytic process |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0009986 | cellular_component | cell surface |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006096 | biological_process | glycolytic process |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| D | 0009986 | cellular_component | cell surface |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 501 |
| Chain | Residue |
| A | LYS344 |
| A | ARG373 |
| A | SER374 |
| A | PO4502 |
| A | HOH2023 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | ARG16 |
| A | ALA41 |
| A | PO4501 |
| A | HOH2023 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 501 |
| Chain | Residue |
| B | GLY40 |
| B | ALA41 |
| B | SER42 |
| B | LYS344 |
| B | ARG373 |
| B | SER374 |
| B | PO4502 |
| B | HOH2022 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 502 |
| Chain | Residue |
| B | GLN163 |
| B | GLU164 |
| B | GLU205 |
| B | ASP243 |
| B | LYS344 |
| B | HIS372 |
| B | SER374 |
| B | LYS395 |
| B | PO4501 |
| B | HOH2073 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 501 |
| Chain | Residue |
| C | GLY40 |
| C | ALA41 |
| C | SER42 |
| C | LYS344 |
| C | ARG373 |
| C | SER374 |
| C | PO4502 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 502 |
| Chain | Residue |
| C | GLU164 |
| C | GLU205 |
| C | LYS344 |
| C | SER371 |
| C | HIS372 |
| C | LYS395 |
| C | PO4501 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 501 |
| Chain | Residue |
| D | LYS344 |
| D | ARG373 |
| D | SER374 |
| D | PO4502 |
| D | HOH2020 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 502 |
| Chain | Residue |
| D | ARG16 |
| D | ALA41 |
| D | SER374 |
| D | PO4501 |
| D | HOH2020 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. ILIKvNQIGTLTET |
| Chain | Residue | Details |
| A | ILE341-THR354 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 |
| Chain | Residue | Details |
| A | GLU205 | |
| B | GLU205 | |
| C | GLU205 | |
| D | GLU205 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 |
| Chain | Residue | Details |
| A | LYS344 | |
| B | LYS344 | |
| C | LYS344 | |
| D | LYS344 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318 |
| Chain | Residue | Details |
| A | GLN163 | |
| B | ASP243 | |
| B | GLU292 | |
| B | ASP319 | |
| B | LYS344 | |
| B | ARG373 | |
| B | SER374 | |
| B | LYS395 | |
| C | GLN163 | |
| C | ASP243 | |
| C | GLU292 | |
| A | ASP243 | |
| C | ASP319 | |
| C | LYS344 | |
| C | ARG373 | |
| C | SER374 | |
| C | LYS395 | |
| D | GLN163 | |
| D | ASP243 | |
| D | GLU292 | |
| D | ASP319 | |
| D | LYS344 | |
| A | GLU292 | |
| D | ARG373 | |
| D | SER374 | |
| D | LYS395 | |
| A | ASP319 | |
| A | LYS344 | |
| A | ARG373 | |
| A | SER374 | |
| A | LYS395 | |
| B | GLN163 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | SITE: Important for binding of plasminogen => ECO:0000269|PubMed:14688086 |
| Chain | Residue | Details |
| A | LYS428 | |
| D | LYS428 | |
| D | LYS434 | |
| D | LYS435 | |
| A | LYS434 | |
| A | LYS435 | |
| B | LYS428 | |
| B | LYS434 | |
| B | LYS435 | |
| C | LYS428 | |
| C | LYS434 | |
| C | LYS435 |
