2DBV
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH ASP 32 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NADP+
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0000166 | molecular_function | nucleotide binding |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0005737 | cellular_component | cytoplasm |
O | 0006006 | biological_process | glucose metabolic process |
O | 0006096 | biological_process | glycolytic 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 | 0030554 | molecular_function | adenyl nucleotide binding |
O | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
P | 0000166 | molecular_function | nucleotide binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
P | 0005737 | cellular_component | cytoplasm |
P | 0006006 | biological_process | glucose metabolic process |
P | 0006096 | biological_process | glycolytic 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 | 0030554 | molecular_function | adenyl nucleotide binding |
P | 0050661 | molecular_function | NADP binding |
P | 0051287 | molecular_function | NAD binding |
Q | 0000166 | molecular_function | nucleotide binding |
Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
Q | 0005737 | cellular_component | cytoplasm |
Q | 0006006 | biological_process | glucose metabolic process |
Q | 0006096 | biological_process | glycolytic 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 | 0030554 | molecular_function | adenyl nucleotide binding |
Q | 0050661 | molecular_function | NADP binding |
Q | 0051287 | molecular_function | NAD binding |
R | 0000166 | molecular_function | nucleotide binding |
R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
R | 0005737 | cellular_component | cytoplasm |
R | 0006006 | biological_process | glucose metabolic process |
R | 0006096 | biological_process | glycolytic 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 | 0030554 | molecular_function | adenyl nucleotide binding |
R | 0050661 | molecular_function | NADP binding |
R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 O 338 |
Chain | Residue |
O | THR179 |
O | ARG195 |
O | ARG231 |
O | NDP336 |
O | HOH400 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 O 339 |
Chain | Residue |
O | HOH399 |
O | SER148 |
O | THR208 |
O | GLY209 |
O | ALA210 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 P 338 |
Chain | Residue |
P | THR179 |
P | ASP181 |
P | ARG195 |
P | ARG231 |
P | NDP336 |
P | HOH351 |
P | HOH400 |
P | HOH408 |
P | HOH411 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 P 339 |
Chain | Residue |
P | SER148 |
P | THR208 |
P | GLY209 |
P | ALA210 |
P | HOH349 |
P | HOH387 |
P | HOH424 |
P | HOH427 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 Q 338 |
Chain | Residue |
Q | THR179 |
Q | ASP181 |
Q | ARG231 |
Q | NDP336 |
Q | HOH349 |
Q | HOH396 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 Q 339 |
Chain | Residue |
Q | SER148 |
Q | THR208 |
Q | GLY209 |
Q | ALA210 |
Q | HOH418 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 R 338 |
Chain | Residue |
R | THR179 |
R | ASP181 |
R | ARG195 |
R | ARG231 |
R | NDP336 |
R | HOH356 |
R | HOH405 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 R 339 |
Chain | Residue |
R | SER148 |
R | THR208 |
R | GLY209 |
R | ALA210 |
R | HOH354 |
R | HOH387 |
R | HOH427 |
site_id | AC9 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NDP O 336 |
Chain | Residue |
O | ASN6 |
O | GLY7 |
O | GLY9 |
O | ARG10 |
O | ILE11 |
O | ASN31 |
O | GLY32 |
O | LEU33 |
O | ARG77 |
O | SER95 |
O | THR96 |
O | GLY97 |
O | SER119 |
O | ALA120 |
O | CYS149 |
O | ASN180 |
O | ASN313 |
O | TYR317 |
O | SO4338 |
O | HOH347 |
O | HOH355 |
O | HOH356 |
O | HOH362 |
O | HOH368 |
O | HOH370 |
O | HOH371 |
O | HOH422 |
O | HOH423 |
O | HOH424 |
R | SER188 |
site_id | BC1 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NDP P 336 |
Chain | Residue |
P | GLU314 |
P | SO4338 |
P | HOH351 |
P | HOH352 |
P | HOH353 |
P | HOH360 |
P | HOH365 |
P | HOH371 |
P | HOH376 |
P | HOH390 |
P | HOH435 |
Q | SER188 |
Q | HOH343 |
P | GLY9 |
P | ARG10 |
P | ILE11 |
P | ASN31 |
P | LEU33 |
P | GLU76 |
P | ARG77 |
P | SER95 |
P | THR96 |
P | GLY97 |
P | ARG98 |
P | PHE99 |
P | SER119 |
P | ALA120 |
P | CYS149 |
P | ASN180 |
P | ASN313 |
site_id | BC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NDP Q 336 |
Chain | Residue |
P | SER188 |
Q | PHE8 |
Q | GLY9 |
Q | ARG10 |
Q | ILE11 |
Q | ASN31 |
Q | LEU33 |
Q | ARG77 |
Q | SER95 |
Q | THR96 |
Q | GLY97 |
Q | SER119 |
Q | ALA120 |
Q | ASN180 |
Q | ASN313 |
Q | TYR317 |
Q | SO4338 |
Q | HOH350 |
Q | HOH361 |
Q | HOH362 |
Q | HOH365 |
Q | HOH371 |
Q | HOH375 |
Q | HOH421 |
Q | HOH422 |
Q | HOH423 |
site_id | BC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NDP R 336 |
Chain | Residue |
O | SER188 |
R | GLY7 |
R | PHE8 |
R | GLY9 |
R | ARG10 |
R | ILE11 |
R | ASN31 |
R | GLY32 |
R | LEU33 |
R | ARG77 |
R | SER95 |
R | THR96 |
R | GLY97 |
R | SER119 |
R | ALA120 |
R | CYS149 |
R | ASN180 |
R | ASN313 |
R | TYR317 |
R | SO4338 |
R | HOH356 |
R | HOH357 |
R | HOH366 |
R | HOH367 |
R | HOH375 |
R | HOH381 |
R | HOH432 |
R | HOH433 |
R | HOH434 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
O | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:18480053, ECO:0000305|PubMed:12569100 |
Chain | Residue | Details |
O | THR150 | |
P | THR150 | |
Q | THR150 | |
R | THR150 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | ILE11 | |
P | ALA120 | |
P | ASP181 | |
P | GLU314 | |
Q | ILE11 | |
Q | LEU33 | |
Q | ASP78 | |
Q | ALA120 | |
Q | ASP181 | |
Q | GLU314 | |
R | ILE11 | |
O | LEU33 | |
R | LEU33 | |
R | ASP78 | |
R | ALA120 | |
R | ASP181 | |
R | GLU314 | |
O | ASP78 | |
O | ALA120 | |
O | ASP181 | |
O | GLU314 | |
P | ILE11 | |
P | LEU33 | |
P | ASP78 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | CYS149 | |
R | CYS149 | |
R | ASN180 | |
R | VAL232 | |
O | ASN180 | |
O | VAL232 | |
P | CYS149 | |
P | ASN180 | |
P | VAL232 | |
Q | CYS149 | |
Q | ASN180 | |
Q | VAL232 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | ALA196 | |
P | ALA196 | |
Q | ALA196 | |
R | ALA196 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | GLY209 | |
P | GLY209 | |
Q | GLY209 | |
R | GLY209 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:Q6GIL8 |
Chain | Residue | Details |
O | SER177 | |
P | SER177 | |
Q | SER177 | |
R | SER177 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
O | CYS149 | |
O | HIS176 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
P | CYS149 | |
P | HIS176 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
Q | CYS149 | |
Q | HIS176 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
R | CYS149 | |
R | HIS176 |