3ZLF
Structure of group A Streptococcal enolase K312A 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 | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 436 |
Chain | Residue |
A | GLN163 |
A | HOH2115 |
A | GLU164 |
A | GLU205 |
A | LYS344 |
A | HIS372 |
A | ARG373 |
A | SER374 |
A | LYS395 |
A | PO4437 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 437 |
Chain | Residue |
A | GLY40 |
A | ALA41 |
A | SER42 |
A | LYS344 |
A | ARG373 |
A | SER374 |
A | PO4436 |
A | HOH2028 |
A | HOH2029 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 436 |
Chain | Residue |
B | ARG16 |
B | ALA41 |
B | SER374 |
B | PO4437 |
B | HOH2021 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 437 |
Chain | Residue |
B | LYS344 |
B | ARG373 |
B | SER374 |
B | PO4436 |
B | HOH2021 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 C 436 |
Chain | Residue |
C | GLN163 |
C | GLU164 |
C | GLU205 |
C | LYS344 |
C | HIS372 |
C | ARG373 |
C | SER374 |
C | LYS395 |
C | PO4437 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 C 437 |
Chain | Residue |
C | GLY40 |
C | ALA41 |
C | SER42 |
C | LYS344 |
C | ARG373 |
C | SER374 |
C | PO4436 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 D 436 |
Chain | Residue |
D | GLN163 |
D | GLU164 |
D | GLU205 |
D | ASP243 |
D | LYS344 |
D | HIS372 |
D | SER374 |
D | LYS395 |
D | PO4437 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 D 437 |
Chain | Residue |
D | GLY40 |
D | ALA41 |
D | SER42 |
D | LYS344 |
D | ARG373 |
D | SER374 |
D | PO4436 |
D | HOH2028 |
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 |