2X5K
Structure of an active site mutant of the D-Erythrose-4-Phosphate Dehydrogenase from E. coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0005737 | cellular_component | cytoplasm |
O | 0005829 | cellular_component | cytosol |
O | 0006006 | biological_process | glucose metabolic process |
O | 0008615 | biological_process | pyridoxine biosynthetic process |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
O | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
O | 0048001 | molecular_function | erythrose-4-phosphate dehydrogenase activity |
O | 0051287 | molecular_function | NAD binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
P | 0005737 | cellular_component | cytoplasm |
P | 0005829 | cellular_component | cytosol |
P | 0006006 | biological_process | glucose metabolic process |
P | 0008615 | biological_process | pyridoxine biosynthetic process |
P | 0016491 | molecular_function | oxidoreductase activity |
P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
P | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
P | 0048001 | molecular_function | erythrose-4-phosphate dehydrogenase activity |
P | 0051287 | molecular_function | NAD binding |
Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
Q | 0005737 | cellular_component | cytoplasm |
Q | 0005829 | cellular_component | cytosol |
Q | 0006006 | biological_process | glucose metabolic process |
Q | 0008615 | biological_process | pyridoxine biosynthetic process |
Q | 0016491 | molecular_function | oxidoreductase activity |
Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Q | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
Q | 0048001 | molecular_function | erythrose-4-phosphate dehydrogenase activity |
Q | 0051287 | molecular_function | NAD binding |
R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
R | 0005737 | cellular_component | cytoplasm |
R | 0005829 | cellular_component | cytosol |
R | 0006006 | biological_process | glucose metabolic process |
R | 0008615 | biological_process | pyridoxine biosynthetic process |
R | 0016491 | molecular_function | oxidoreductase activity |
R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
R | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
R | 0048001 | molecular_function | erythrose-4-phosphate dehydrogenase activity |
R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL P 1335 |
Chain | Residue |
P | ASP323 |
P | HOH2022 |
P | HOH2245 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL R 1334 |
Chain | Residue |
R | ALA54 |
R | TRP55 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL R 1335 |
Chain | Residue |
R | HOH2203 |
O | ASN123 |
R | LEU33 |
R | ALA34 |
R | HIS75 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL O 1336 |
Chain | Residue |
O | ALA164 |
O | HOH2147 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL P 1336 |
Chain | Residue |
P | GLU86 |
P | HOH2029 |
P | HOH2246 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO O 1337 |
Chain | Residue |
O | VAL98 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO P 1337 |
Chain | Residue |
P | TRP55 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO R 1336 |
Chain | Residue |
R | HOH2170 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 O 1338 |
Chain | Residue |
O | ALA38 |
O | HOH2257 |
P | ARG142 |
P | ARG334 |
R | LEU193 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL P 1338 |
Chain | Residue |
P | THR48 |
Q | ARG197 |
Q | ALA198 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL O 1339 |
Chain | Residue |
O | THR48 |
R | ARG197 |
R | ALA198 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL Q 1339 |
Chain | Residue |
P | ARG197 |
P | ALA198 |
Q | THR48 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG P 1340 |
Chain | Residue |
P | ARG58 |
P | GLU60 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PEG P 1341 |
Chain | Residue |
Q | LEU193 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGE O 1340 |
Chain | Residue |
O | GLN264 |
O | HIS268 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGE P 1342 |
Chain | Residue |
P | GLU103 |
P | ALA110 |
P | HOH2109 |
R | TYR188 |
R | HIS190 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGE Q 1336 |
Chain | Residue |
Q | GLY97 |
Q | VAL98 |
Q | GLY100 |
Q | HIS120 |
Q | SER122 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGE P 1343 |
Chain | Residue |
P | VAL98 |
P | TYR99 |
P | HIS104 |
R | HOH2075 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
O | ALA149 | |
P | ALA149 | |
Q | ALA149 | |
R | ALA149 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
O | ARG10 | |
R | ARG10 | |
R | ARG77 | |
R | ASN313 | |
O | ARG77 | |
O | ASN313 | |
P | ARG10 | |
P | ARG77 | |
P | ASN313 | |
Q | ARG10 | |
Q | ARG77 | |
Q | ASN313 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
O | SER148 | |
Q | ARG195 | |
Q | THR208 | |
Q | ARG231 | |
R | SER148 | |
R | ARG195 | |
R | THR208 | |
R | ARG231 | |
O | ARG195 | |
O | THR208 | |
O | ARG231 | |
P | SER148 | |
P | ARG195 | |
P | THR208 | |
P | ARG231 | |
Q | SER148 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250 |
Chain | Residue | Details |
O | HIS176 | |
P | HIS176 | |
Q | HIS176 | |
R | HIS176 |