3UJ2
CRYSTAL STRUCTURE OF AN ENOLASE FROM ANAEROSTIPES CACCAE (EFI TARGET EFI-502054) WITH BOUND MG AND SULFATE
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 |
E | 0000015 | cellular_component | phosphopyruvate hydratase complex |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0004634 | molecular_function | phosphopyruvate hydratase activity |
E | 0005576 | cellular_component | extracellular region |
E | 0005737 | cellular_component | cytoplasm |
E | 0006096 | biological_process | glycolytic process |
E | 0009986 | cellular_component | cell surface |
E | 0016829 | molecular_function | lyase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0000015 | cellular_component | phosphopyruvate hydratase complex |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0004634 | molecular_function | phosphopyruvate hydratase activity |
F | 0005576 | cellular_component | extracellular region |
F | 0005737 | cellular_component | cytoplasm |
F | 0006096 | biological_process | glycolytic process |
F | 0009986 | cellular_component | cell surface |
F | 0016829 | molecular_function | lyase activity |
F | 0046872 | molecular_function | metal ion binding |
G | 0000015 | cellular_component | phosphopyruvate hydratase complex |
G | 0000287 | molecular_function | magnesium ion binding |
G | 0004634 | molecular_function | phosphopyruvate hydratase activity |
G | 0005576 | cellular_component | extracellular region |
G | 0005737 | cellular_component | cytoplasm |
G | 0006096 | biological_process | glycolytic process |
G | 0009986 | cellular_component | cell surface |
G | 0016829 | molecular_function | lyase activity |
G | 0046872 | molecular_function | metal ion binding |
H | 0000015 | cellular_component | phosphopyruvate hydratase complex |
H | 0000287 | molecular_function | magnesium ion binding |
H | 0004634 | molecular_function | phosphopyruvate hydratase activity |
H | 0005576 | cellular_component | extracellular region |
H | 0005737 | cellular_component | cytoplasm |
H | 0006096 | biological_process | glycolytic process |
H | 0009986 | cellular_component | cell surface |
H | 0016829 | molecular_function | lyase activity |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 428 |
Chain | Residue |
A | GLY42 |
A | ARG370 |
A | SER371 |
A | HOH533 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 429 |
Chain | Residue |
A | ARG178 |
A | GLU179 |
A | ARG182 |
B | ARG60 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 430 |
Chain | Residue |
A | ASN20 |
A | LYS64 |
A | HOH790 |
A | HOH1368 |
B | HIS189 |
A | ARG18 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 431 |
Chain | Residue |
A | ASP244 |
A | GLU289 |
A | ASP316 |
A | HOH442 |
A | HOH470 |
A | HOH1536 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 428 |
Chain | Residue |
A | ARG60 |
B | GLU179 |
B | ARG182 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 429 |
Chain | Residue |
B | GLY42 |
B | ARG370 |
B | SER371 |
B | HOH745 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 430 |
Chain | Residue |
A | HOH684 |
B | ARG18 |
B | ASN20 |
B | LYS64 |
B | HOH479 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 431 |
Chain | Residue |
B | ASP244 |
B | GLU289 |
B | ASP316 |
B | HOH962 |
B | HOH1542 |
B | HOH1543 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 428 |
Chain | Residue |
C | GLY42 |
C | ARG370 |
C | SER371 |
C | HOH1570 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 429 |
Chain | Residue |
C | ARG178 |
C | GLU179 |
C | ARG182 |
D | ARG60 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 430 |
Chain | Residue |
C | GLU218 |
C | ARG265 |
C | ARG265 |
C | HIS275 |
C | SER278 |
C | ARG282 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 431 |
Chain | Residue |
C | ASP244 |
C | GLU289 |
C | ASP316 |
C | HOH482 |
C | HOH958 |
C | HOH968 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 428 |
Chain | Residue |
C | ARG60 |
D | ARG178 |
D | GLU179 |
D | ARG182 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 429 |
Chain | Residue |
D | GLY42 |
D | ARG370 |
D | SER371 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 430 |
Chain | Residue |
D | ASP244 |
D | GLU289 |
D | ASP316 |
D | HOH431 |
D | HOH453 |
D | HOH1584 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 428 |
Chain | Residue |
E | GLY42 |
E | LYS341 |
E | ARG370 |
E | SER371 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 429 |
Chain | Residue |
E | ARG178 |
E | GLU179 |
E | ARG182 |
F | ARG60 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG E 430 |
Chain | Residue |
E | GLN165 |
E | ASP244 |
E | GLU289 |
E | ASP316 |
E | HOH443 |
E | HOH1233 |
E | HOH1612 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 428 |
Chain | Residue |
E | ARG60 |
F | ARG178 |
F | GLU179 |
F | ARG182 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 F 429 |
Chain | Residue |
F | GLY42 |
F | ARG370 |
F | SER371 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG F 430 |
Chain | Residue |
F | ASP244 |
F | GLU289 |
F | ASP316 |
F | HOH432 |
F | HOH961 |
F | HOH1621 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 G 428 |
Chain | Residue |
G | ARG178 |
G | GLU179 |
G | ARG182 |
H | ARG60 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 G 429 |
Chain | Residue |
G | ARG18 |
G | ASN20 |
G | LYS64 |
G | HOH521 |
H | HIS189 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 430 |
Chain | Residue |
G | GLY42 |
G | ARG370 |
G | SER371 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG G 431 |
Chain | Residue |
G | ASP244 |
G | GLU289 |
G | ASP316 |
G | HOH439 |
G | HOH1220 |
G | HOH1228 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 H 428 |
Chain | Residue |
H | GLY42 |
H | ARG370 |
H | SER371 |
H | HOH1264 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 H 429 |
Chain | Residue |
G | ARG60 |
H | GLU179 |
H | ARG182 |
site_id | DC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG H 430 |
Chain | Residue |
H | GLN165 |
H | ASP244 |
H | GLU289 |
H | ASP316 |
H | HOH980 |
H | HOH1649 |
Functional Information from PROSITE/UniProt
site_id | PS00164 |
Number of Residues | 14 |
Details | ENOLASE Enolase signature. ILIKlNQIGTVSET |
Chain | Residue | Details |
A | ILE338-THR351 |