1IHX
Crystal structure of two D-glyceraldehyde-3-phosphate dehydrogenase complexes: a case of asymmetry
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | SER148 |
A | THR208 |
A | GLY209 |
A | ALA210 |
A | HOH562 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 502 |
Chain | Residue |
B | ALA210 |
B | HOH563 |
B | SER148 |
B | THR150 |
B | THR208 |
B | GLY209 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 503 |
Chain | Residue |
C | SER148 |
C | THR208 |
C | GLY209 |
C | ALA210 |
C | HOH555 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 504 |
Chain | Residue |
D | SER148 |
D | THR150 |
D | THR208 |
D | GLY209 |
D | ALA210 |
D | HOH552 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | THR179 |
A | THR181 |
A | ARG231 |
A | SND335 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 506 |
Chain | Residue |
B | THR179 |
B | THR181 |
B | ARG231 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 507 |
Chain | Residue |
C | THR179 |
C | THR181 |
C | ARG231 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 508 |
Chain | Residue |
D | THR179 |
D | THR181 |
D | ARG231 |
D | SND338 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE SND A 335 |
Chain | Residue |
A | ASN6 |
A | GLY7 |
A | PHE8 |
A | GLY9 |
A | ARG10 |
A | ILE11 |
A | ASP32 |
A | PRO33 |
A | PHE34 |
A | ILE35 |
A | MET77 |
A | SER95 |
A | THR96 |
A | SER119 |
A | ALA120 |
A | SO4505 |
A | HOH506 |
A | HOH559 |
A | HOH560 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SND B 336 |
Chain | Residue |
B | ASN6 |
B | GLY7 |
B | PHE8 |
B | GLY9 |
B | ARG10 |
B | ILE11 |
B | ASN31 |
B | ASP32 |
B | PRO33 |
B | PHE34 |
B | ILE35 |
B | MET77 |
B | THR96 |
B | GLY97 |
B | PHE99 |
B | SER119 |
B | ALA120 |
B | HOH509 |
B | HOH531 |
B | HOH572 |
site_id | BC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SND C 337 |
Chain | Residue |
C | ASN6 |
C | GLY7 |
C | GLY9 |
C | ARG10 |
C | ILE11 |
C | ASN31 |
C | ASP32 |
C | PRO33 |
C | PHE34 |
C | ILE35 |
C | MET77 |
C | SER95 |
C | THR96 |
C | GLY97 |
C | PHE99 |
C | SER119 |
C | CYS149 |
C | ASN313 |
C | TYR317 |
C | HOH547 |
site_id | BC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE SND D 338 |
Chain | Residue |
D | ARG10 |
D | ILE11 |
D | ASN31 |
D | ASP32 |
D | PRO33 |
D | PHE34 |
D | MET77 |
D | THR96 |
D | GLY97 |
D | PHE99 |
D | SER119 |
D | ALA120 |
D | CYS149 |
D | ASN313 |
D | SO4508 |
D | HOH511 |
D | HOH515 |
D | HOH538 |
D | HOH542 |
B | HOH555 |
D | ASN6 |
D | PHE8 |
D | GLY9 |
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 | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | CYS149 | |
B | CYS149 | |
C | CYS149 | |
D | CYS149 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9761850 |
Chain | Residue | Details |
A | ARG10 | |
D | ARG10 | |
D | ASP32 | |
D | ASN313 | |
A | ASP32 | |
A | ASN313 | |
B | ARG10 | |
B | ASP32 | |
B | ASN313 | |
C | ARG10 | |
C | ASP32 | |
C | ASN313 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | MET77 | |
B | ARG231 | |
C | MET77 | |
C | SER148 | |
C | THR179 | |
C | THR208 | |
C | ARG231 | |
D | MET77 | |
D | SER148 | |
D | THR179 | |
D | THR208 | |
A | SER148 | |
D | ARG231 | |
A | THR179 | |
A | THR208 | |
A | ARG231 | |
B | MET77 | |
B | SER148 | |
B | THR179 | |
B | THR208 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis |
Chain | Residue | Details |
A | HIS176 | |
B | HIS176 | |
C | HIS176 | |
D | HIS176 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P00357 |
Chain | Residue | Details |
A | SER1 | |
B | SER1 | |
C | SER1 | |
D | SER1 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
A | CYS149 | |
A | HIS176 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
B | CYS149 | |
B | HIS176 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
C | CYS149 | |
C | HIS176 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
D | CYS149 | |
D | HIS176 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 911 |
Chain | Residue | Details |
A | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
A | HIS176 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 911 |
Chain | Residue | Details |
B | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
B | HIS176 | proton shuttle (general acid/base) |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 911 |
Chain | Residue | Details |
C | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
C | HIS176 | proton shuttle (general acid/base) |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 911 |
Chain | Residue | Details |
D | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
D | HIS176 | proton shuttle (general acid/base) |