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 | 0005576 | cellular_component | extracellular region |
A | 0005737 | cellular_component | cytoplasm |
A | 0006096 | biological_process | glycolytic process |
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 | 0005576 | cellular_component | extracellular region |
B | 0005737 | cellular_component | cytoplasm |
B | 0006096 | biological_process | glycolytic process |
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 | 0005576 | cellular_component | extracellular region |
C | 0005737 | cellular_component | cytoplasm |
C | 0006096 | biological_process | glycolytic process |
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 | 0005576 | cellular_component | extracellular region |
D | 0005737 | cellular_component | cytoplasm |
D | 0006096 | biological_process | glycolytic process |
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 | 6 |
Details | BINDING SITE FOR RESIDUE MG A 601 |
Chain | Residue |
A | ASP239 |
A | GLU280 |
A | ASP307 |
A | HOH467 |
A | HOH545 |
A | HOH572 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | HOH416 |
B | HOH452 |
B | HOH567 |
B | ASP239 |
B | GLU280 |
B | ASP307 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 601 |
Chain | Residue |
C | ASP239 |
C | GLU280 |
C | ASP307 |
C | HOH446 |
C | HOH544 |
C | HOH568 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 601 |
Chain | Residue |
D | ASP239 |
D | GLU280 |
D | ASP307 |
D | HOH439 |
D | HOH459 |
D | HOH475 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD C 415 |
Chain | Residue |
C | LYS22 |
C | ALA35 |
C | ARG119 |
C | ASP367 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD D 602 |
Chain | Residue |
D | LYS22 |
D | ARG119 |
D | GLU366 |
D | ASP367 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD B 603 |
Chain | Residue |
A | GOL605 |
B | LYS22 |
B | ALA34 |
B | GLU366 |
B | ASP367 |
B | HOH422 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 604 |
Chain | Residue |
A | LYS22 |
A | ALA34 |
A | ASP367 |
A | HOH427 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 605 |
Chain | Residue |
A | ALA368 |
A | ALA394 |
A | GLU401 |
B | LYS22 |
B | ILE36 |
B | GLU366 |
B | MPD603 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 606 |
Chain | Residue |
C | SER195 |
C | HIS197 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 607 |
Chain | Residue |
C | ALA394 |
C | ASN397 |
C | ARG398 |
C | GLU401 |
C | HOH471 |
D | LYS22 |
D | ILE36 |
D | GLU366 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 608 |
Chain | Residue |
D | GLY299 |
D | LYS301 |
D | ILE302 |
D | GLN303 |
D | ASN327 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 609 |
Chain | Residue |
B | GLY299 |
B | ASN300 |
B | LYS301 |
B | ILE302 |
B | GLN303 |
B | ASN327 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 610 |
Chain | Residue |
C | GLY299 |
C | ASN300 |
C | ILE302 |
C | GLN303 |
Functional Information from PROSITE/UniProt
site_id | PS00164 |
Number of Residues | 14 |
Details | ENOLASE Enolase signature. VLIKpNQIGTITQT |
Chain | Residue | Details |
A | VAL329-THR342 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU204 | |
B | GLU204 | |
C | GLU204 | |
D | GLU204 | |
Chain | Residue | Details |
A | LYS332 | |
B | LYS332 | |
C | LYS332 | |
D | LYS332 | |
Chain | Residue | Details |
A | GLN162 | |
B | LYS383 | |
C | GLN162 | |
C | LYS332 | |
C | ARG361 | |
C | SER362 | |
C | LYS383 | |
D | GLN162 | |
D | LYS332 | |
D | ARG361 | |
D | SER362 | |
A | LYS332 | |
D | LYS383 | |
A | ARG361 | |
A | SER362 | |
A | LYS383 | |
B | GLN162 | |
B | LYS332 | |
B | ARG361 | |
B | SER362 | |
Chain | Residue | Details |
A | ASP239 | |
D | ASP239 | |
D | GLU280 | |
D | ASP307 | |
A | GLU280 | |
A | ASP307 | |
B | ASP239 | |
B | GLU280 | |
B | ASP307 | |
C | ASP239 | |
C | GLU280 | |
C | ASP307 | |