3CIF
Crystal Structure of C153S mutant glyceraldehyde 3-phosphate dehydrogenase from Cryptosporidium parvum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006006 | biological_process | glucose metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006006 | biological_process | glucose metabolic process |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE G3H A 1337 |
| Chain | Residue |
| A | SER152 |
| A | ASN319 |
| A | HOH407 |
| A | HOH423 |
| A | HOH491 |
| A | HOH699 |
| A | NAD5463 |
| A | SER153 |
| A | THR154 |
| A | HIS180 |
| A | THR183 |
| A | THR214 |
| A | GLY215 |
| A | ALA216 |
| A | ARG237 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE G3H B 1338 |
| Chain | Residue |
| B | SER152 |
| B | SER153 |
| B | THR154 |
| B | HIS180 |
| B | THR183 |
| B | THR214 |
| B | GLY215 |
| B | ALA216 |
| B | ARG237 |
| B | HOH364 |
| B | HOH412 |
| B | HOH634 |
| B | HOH700 |
| B | NAD5464 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3H D 1340 |
| Chain | Residue |
| D | SER152 |
| D | SER153 |
| D | THR154 |
| D | HIS180 |
| D | ARG237 |
| D | MG340 |
| D | HOH384 |
| D | HOH430 |
| D | NAD5466 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 5463 |
| Chain | Residue |
| A | ASN8 |
| A | GLY9 |
| A | GLY11 |
| A | ARG12 |
| A | ILE13 |
| A | ASN33 |
| A | ASP34 |
| A | PRO35 |
| A | PHE36 |
| A | MET37 |
| A | ALA78 |
| A | LYS79 |
| A | SER97 |
| A | THR98 |
| A | GLY99 |
| A | PHE101 |
| A | SER121 |
| A | ALA122 |
| A | ALA184 |
| A | ASN319 |
| A | TYR323 |
| A | HOH340 |
| A | HOH343 |
| A | HOH346 |
| A | HOH350 |
| A | HOH356 |
| A | HOH386 |
| A | HOH408 |
| A | HOH446 |
| A | HOH453 |
| A | G3H1337 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD B 5464 |
| Chain | Residue |
| B | HOH548 |
| B | HOH720 |
| B | G3H1338 |
| C | HOH410 |
| B | ASN8 |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN33 |
| B | ASP34 |
| B | PRO35 |
| B | PHE36 |
| B | MET37 |
| B | ALA78 |
| B | LYS79 |
| B | SER97 |
| B | THR98 |
| B | GLY99 |
| B | PHE101 |
| B | SER121 |
| B | ALA122 |
| B | ALA184 |
| B | ASN319 |
| B | TYR323 |
| B | HOH342 |
| B | HOH345 |
| B | HOH346 |
| B | HOH348 |
| B | HOH355 |
| B | HOH356 |
| B | HOH369 |
| B | HOH373 |
| B | HOH394 |
| site_id | AC6 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD C 5465 |
| Chain | Residue |
| C | ASN8 |
| C | GLY9 |
| C | GLY11 |
| C | ARG12 |
| C | ILE13 |
| C | ASN33 |
| C | ASP34 |
| C | PRO35 |
| C | PHE36 |
| C | MET37 |
| C | ALA78 |
| C | LYS79 |
| C | SER97 |
| C | THR98 |
| C | GLY99 |
| C | PHE101 |
| C | SER121 |
| C | ALA122 |
| C | ALA184 |
| C | ASN319 |
| C | TYR323 |
| C | GOL340 |
| C | HOH347 |
| C | HOH350 |
| C | HOH358 |
| C | HOH365 |
| C | HOH372 |
| C | HOH388 |
| C | HOH393 |
| C | HOH440 |
| C | HOH484 |
| C | HOH704 |
| C | HOH705 |
| C | HOH706 |
| C | G3H1339 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD D 5466 |
| Chain | Residue |
| D | ASN8 |
| D | GLY9 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASN33 |
| D | ASP34 |
| D | PRO35 |
| D | PHE36 |
| D | MET37 |
| D | ALA78 |
| D | LYS79 |
| D | SER97 |
| D | THR98 |
| D | GLY99 |
| D | PHE101 |
| D | SER121 |
| D | ALA122 |
| D | ALA184 |
| D | ASN319 |
| D | TYR323 |
| D | HOH354 |
| D | HOH355 |
| D | HOH369 |
| D | HOH370 |
| D | HOH371 |
| D | HOH384 |
| D | HOH423 |
| D | HOH430 |
| D | HOH438 |
| D | HOH483 |
| D | G3H1340 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 340 |
| Chain | Residue |
| C | PHE36 |
| C | HOH544 |
| C | NAD5465 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 340 |
| Chain | Residue |
| B | ASP288 |
| B | CYS292 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 341 |
| Chain | Residue |
| B | CYS21 |
| B | ARG24 |
| B | ILE27 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE G3H C 1339 |
| Chain | Residue |
| C | SER152 |
| C | SER153 |
| C | THR154 |
| C | HIS180 |
| C | THR183 |
| C | THR214 |
| C | ALA216 |
| C | ARG237 |
| C | HOH527 |
| C | HOH687 |
| C | HOH701 |
| C | HOH702 |
| C | NAD5465 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 340 |
| Chain | Residue |
| D | THR154 |
| D | THR214 |
| D | HOH342 |
| D | G3H1340 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| A | HIS180 | |
| A | SER153 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | HIS180 | |
| B | SER153 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | HIS180 | |
| C | SER153 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| D | HIS180 | |
| D | SER153 |
