3HJA
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Borrelia burgdorferi
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 | 0005737 | cellular_component | cytoplasm |
| 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 | 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 336 |
| Chain | Residue |
| A | SER152 |
| A | CYS153 |
| A | THR154 |
| A | HIS180 |
| A | THR211 |
| A | ARG234 |
| A | HOH408 |
| A | HOH411 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 337 |
| Chain | Residue |
| A | GLY9 |
| A | ARG10 |
| A | ILE11 |
| A | ASN30 |
| A | ASP31 |
| A | LEU32 |
| A | ARG75 |
| A | SER93 |
| A | THR94 |
| A | GLY95 |
| A | PHE97 |
| A | THR122 |
| A | VAL123 |
| A | ASN184 |
| A | ASN318 |
| A | TYR322 |
| A | SO4338 |
| A | HOH342 |
| A | HOH358 |
| A | HOH385 |
| A | HOH397 |
| A | HOH439 |
| A | HOH447 |
| A | HOH573 |
| A | HOH599 |
| A | HOH757 |
| A | HOH758 |
| A | HOH759 |
| B | LEU191 |
| B | HOH354 |
| A | GLY7 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 338 |
| Chain | Residue |
| A | THR183 |
| A | ASP185 |
| A | ARG198 |
| A | ARG234 |
| A | NAD337 |
| A | HOH358 |
| A | HOH411 |
| A | HOH776 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 339 |
| Chain | Residue |
| A | LYS215 |
| A | ASN229 |
| A | HOH359 |
| A | HOH446 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 336 |
| Chain | Residue |
| B | SER152 |
| B | CYS153 |
| B | THR154 |
| B | HIS180 |
| B | THR211 |
| B | ARG234 |
| B | HOH372 |
| B | HOH471 |
| B | HOH769 |
| site_id | AC6 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD B 337 |
| Chain | Residue |
| A | LEU191 |
| A | HOH346 |
| B | GLY7 |
| B | GLY9 |
| B | ARG10 |
| B | ILE11 |
| B | ASN30 |
| B | ASP31 |
| B | LEU32 |
| B | ARG75 |
| B | SER93 |
| B | THR94 |
| B | GLY95 |
| B | PHE97 |
| B | THR122 |
| B | VAL123 |
| B | ASN184 |
| B | ASN318 |
| B | TYR322 |
| B | SO4338 |
| B | HOH347 |
| B | HOH352 |
| B | HOH363 |
| B | HOH368 |
| B | HOH396 |
| B | HOH423 |
| B | HOH430 |
| B | HOH466 |
| B | HOH472 |
| B | HOH614 |
| B | HOH761 |
| B | HOH762 |
| B | HOH763 |
| B | HOH764 |
| B | HOH784 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 338 |
| Chain | Residue |
| B | NAD337 |
| B | HOH368 |
| B | HOH471 |
| B | HOH589 |
| B | THR183 |
| B | ASP185 |
| B | ARG198 |
| B | ARG234 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 339 |
| Chain | Residue |
| B | LYS215 |
| B | ASN229 |
| B | HOH348 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 336 |
| Chain | Residue |
| C | SER152 |
| C | CYS153 |
| C | THR154 |
| C | THR211 |
| C | ARG234 |
| C | HOH419 |
| C | HOH424 |
| site_id | BC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD C 337 |
| Chain | Residue |
| C | GLY7 |
| C | GLY9 |
| C | ARG10 |
| C | ILE11 |
| C | ASN30 |
| C | ASP31 |
| C | LEU32 |
| C | ARG75 |
| C | SER93 |
| C | THR94 |
| C | GLY95 |
| C | PHE97 |
| C | THR122 |
| C | VAL123 |
| C | ASN184 |
| C | ASN318 |
| C | TYR322 |
| C | SO4338 |
| C | HOH340 |
| C | HOH351 |
| C | HOH364 |
| C | HOH365 |
| C | HOH366 |
| C | HOH372 |
| C | HOH391 |
| C | HOH400 |
| C | HOH426 |
| C | HOH721 |
| C | HOH774 |
| C | HOH855 |
| D | LEU191 |
| D | HOH359 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 338 |
| Chain | Residue |
| C | THR183 |
| C | ASP185 |
| C | ARG198 |
| C | ARG234 |
| C | NAD337 |
| C | HOH400 |
| C | HOH857 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 339 |
| Chain | Residue |
| B | MET303 |
| C | LYS215 |
| C | ASN229 |
| C | HOH466 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 D 336 |
| Chain | Residue |
| D | SER152 |
| D | CYS153 |
| D | THR154 |
| D | HIS180 |
| D | THR211 |
| D | ARG234 |
| D | HOH390 |
| D | HOH419 |
| D | HOH603 |
| site_id | BC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD D 337 |
| Chain | Residue |
| C | LEU191 |
| C | HOH352 |
| D | GLY7 |
| D | GLY9 |
| D | ARG10 |
| D | ILE11 |
| D | ASN30 |
| D | ASP31 |
| D | LEU32 |
| D | ARG75 |
| D | SER93 |
| D | THR94 |
| D | GLY95 |
| D | PHE97 |
| D | THR122 |
| D | VAL123 |
| D | ASN184 |
| D | ASN318 |
| D | TYR322 |
| D | SO4338 |
| D | HOH347 |
| D | HOH348 |
| D | HOH350 |
| D | HOH375 |
| D | HOH384 |
| D | HOH386 |
| D | HOH387 |
| D | HOH394 |
| D | HOH427 |
| D | HOH562 |
| D | HOH753 |
| D | HOH754 |
| D | HOH755 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 338 |
| Chain | Residue |
| D | THR183 |
| D | ASP185 |
| D | ARG198 |
| D | ARG234 |
| D | NAD337 |
| D | HOH375 |
| D | HOH848 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 339 |
| Chain | Residue |
| A | MET303 |
| D | LYS215 |
| D | ASN229 |
| D | HOH701 |
| D | HOH750 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| A | ALA151-LEU158 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|Ref.3 |
| Chain | Residue | Details |
| A | CYS153 | |
| B | CYS153 | |
| C | CYS153 | |
| D | CYS153 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | BINDING: BINDING => ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | ARG10 | |
| A | ARG234 | |
| A | ASN318 | |
| B | ARG10 | |
| B | ASP31 | |
| B | ARG75 | |
| B | THR122 | |
| B | SER152 | |
| B | THR183 | |
| B | ASN184 | |
| B | ARG198 | |
| A | ASP31 | |
| B | THR211 | |
| B | ARG234 | |
| B | ASN318 | |
| C | ARG10 | |
| C | ASP31 | |
| C | ARG75 | |
| C | THR122 | |
| C | SER152 | |
| C | THR183 | |
| C | ASN184 | |
| A | ARG75 | |
| C | ARG198 | |
| C | THR211 | |
| C | ARG234 | |
| C | ASN318 | |
| D | ARG10 | |
| D | ASP31 | |
| D | ARG75 | |
| D | THR122 | |
| D | SER152 | |
| D | THR183 | |
| A | THR122 | |
| D | ASN184 | |
| D | ARG198 | |
| D | THR211 | |
| D | ARG234 | |
| D | ASN318 | |
| A | SER152 | |
| A | THR183 | |
| A | ASN184 | |
| A | ARG198 | |
| A | THR211 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P00362 |
| Chain | Residue | Details |
| A | HIS180 | |
| B | HIS180 | |
| C | HIS180 | |
| D | HIS180 |
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 | CYS153 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | HIS180 | |
| B | CYS153 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | HIS180 | |
| C | CYS153 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| D | HIS180 | |
| D | CYS153 |
