3B20
Crystal structure of Glyceraldehyde-3-Phosphate Dehydrogenase complexed with NADfrom Synechococcus elongatus"
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 | 0006006 | biological_process | glucose metabolic 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 | 0046872 | molecular_function | metal ion 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 | 0006006 | biological_process | glucose metabolic 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 | 0046872 | molecular_function | metal ion binding |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
O | 0000166 | molecular_function | nucleotide binding |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0006006 | biological_process | glucose metabolic 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 | 0046872 | molecular_function | metal ion 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 | 0006006 | biological_process | glucose metabolic 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 | 0046872 | molecular_function | metal ion 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 | 0006006 | biological_process | glucose metabolic 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 | 0046872 | molecular_function | metal ion 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 | 0006006 | biological_process | glucose metabolic 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 | 0046872 | molecular_function | metal ion binding |
R | 0050661 | molecular_function | NADP binding |
R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1339 |
Chain | Residue |
A | SER154 |
A | THR156 |
A | THR213 |
A | GLY214 |
A | ALA215 |
A | HOH361 |
A | HOH380 |
A | HOH399 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1340 |
Chain | Residue |
A | ASP187 |
A | ARG200 |
A | ARG236 |
A | NAD340 |
A | THR185 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD A 340 |
Chain | Residue |
A | GLY9 |
A | GLY11 |
A | ARG12 |
A | ILE13 |
A | ASN35 |
A | ASN36 |
A | THR37 |
A | ARG80 |
A | SER98 |
A | THR99 |
A | GLY100 |
A | THR122 |
A | ALA123 |
A | CYS155 |
A | LEU186 |
A | ASN318 |
A | HOH352 |
A | HOH404 |
A | HOH417 |
A | HOH422 |
A | SO41340 |
B | HOH413 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 2339 |
Chain | Residue |
B | SER154 |
B | THR213 |
B | GLY214 |
B | ALA215 |
B | HOH347 |
B | HOH377 |
B | HOH442 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 2340 |
Chain | Residue |
B | THR185 |
B | ASP187 |
B | ARG200 |
B | ARG236 |
B | NAD340 |
B | HOH374 |
B | HOH377 |
site_id | AC6 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD B 340 |
Chain | Residue |
B | GLY9 |
B | PHE10 |
B | GLY11 |
B | ARG12 |
B | ILE13 |
B | ASN35 |
B | ASN36 |
B | THR37 |
B | ARG80 |
B | THR99 |
B | GLY100 |
B | THR122 |
B | ALA123 |
B | CYS155 |
B | LEU186 |
B | ASN318 |
B | TYR322 |
B | HOH374 |
B | HOH378 |
B | HOH412 |
B | HOH418 |
B | HOH419 |
B | HOH436 |
B | SO42340 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 O 3339 |
Chain | Residue |
O | SER154 |
O | THR156 |
O | THR213 |
O | GLY214 |
O | ALA215 |
O | HOH362 |
O | HOH397 |
O | HOH419 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 O 3340 |
Chain | Residue |
O | THR185 |
O | ASP187 |
O | ARG200 |
O | ARG236 |
O | NAD340 |
site_id | AC9 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD O 340 |
Chain | Residue |
O | LEU186 |
O | ASN318 |
O | GLU319 |
O | HOH389 |
O | HOH410 |
O | HOH413 |
O | HOH417 |
O | SO43340 |
O | PHE10 |
O | GLY11 |
O | ARG12 |
O | ILE13 |
O | ASN36 |
O | THR37 |
O | ARG80 |
O | SER98 |
O | THR99 |
O | GLY100 |
O | THR122 |
O | ALA123 |
O | CYS155 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 P 4339 |
Chain | Residue |
P | SER154 |
P | THR156 |
P | THR213 |
P | GLY214 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 P 4340 |
Chain | Residue |
P | THR185 |
P | ASP187 |
P | ARG200 |
P | ARG236 |
P | NAD340 |
P | HOH398 |
site_id | BC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD P 340 |
Chain | Residue |
P | GLY9 |
P | PHE10 |
P | GLY11 |
P | ARG12 |
P | ILE13 |
P | ASN35 |
P | ASN36 |
P | THR37 |
P | ARG80 |
P | THR99 |
P | GLY100 |
P | THR122 |
P | ALA123 |
P | CYS155 |
P | THR185 |
P | LEU186 |
P | ASN318 |
P | GLU319 |
P | TYR322 |
P | HOH371 |
P | HOH382 |
P | HOH388 |
P | SO44340 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 Q 5339 |
Chain | Residue |
Q | SER154 |
Q | THR156 |
Q | THR213 |
Q | GLY214 |
Q | ALA215 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 Q 5340 |
Chain | Residue |
Q | THR185 |
Q | ASP187 |
Q | ARG200 |
Q | ARG236 |
Q | NAD340 |
site_id | BC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAD Q 340 |
Chain | Residue |
Q | GLY9 |
Q | GLY11 |
Q | ARG12 |
Q | ILE13 |
Q | ASN35 |
Q | THR37 |
Q | ARG80 |
Q | SER98 |
Q | THR99 |
Q | GLY100 |
Q | THR122 |
Q | ALA123 |
Q | CYS155 |
Q | THR185 |
Q | LEU186 |
Q | ASN318 |
Q | GLU319 |
Q | HOH357 |
Q | SO45340 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 R 6339 |
Chain | Residue |
R | SER154 |
R | THR213 |
R | ALA215 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 R 6340 |
Chain | Residue |
R | THR185 |
R | ARG200 |
R | ARG236 |
R | NAD340 |
site_id | BC9 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD R 340 |
Chain | Residue |
R | GLY9 |
R | GLY11 |
R | ARG12 |
R | ILE13 |
R | THR37 |
R | ARG80 |
R | SER98 |
R | THR99 |
R | GLY100 |
R | THR122 |
R | ALA123 |
R | CYS155 |
R | THR185 |
R | LEU186 |
R | ASN318 |
R | GLU319 |
R | TYR322 |
R | HOH357 |
R | HOH365 |
R | SO46340 |
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 | ALA153-LEU160 |