1PSD
THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004617 | molecular_function | phosphoglycerate dehydrogenase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006564 | biological_process | L-serine biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0042802 | molecular_function | identical protein binding |
A | 0047545 | molecular_function | 2-hydroxyglutarate dehydrogenase activity |
A | 0051287 | molecular_function | NAD binding |
A | 0070403 | molecular_function | NAD+ binding |
A | 0070404 | molecular_function | NADH binding |
A | 0070905 | molecular_function | serine binding |
B | 0004617 | molecular_function | phosphoglycerate dehydrogenase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006564 | biological_process | L-serine biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0042802 | molecular_function | identical protein binding |
B | 0047545 | molecular_function | 2-hydroxyglutarate dehydrogenase activity |
B | 0051287 | molecular_function | NAD binding |
B | 0070403 | molecular_function | NAD+ binding |
B | 0070404 | molecular_function | NADH binding |
B | 0070905 | molecular_function | serine binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD A 450 |
Chain | Residue |
A | PHE106 |
A | ASN108 |
A | GLY160 |
A | HIS161 |
A | ILE162 |
A | ASP181 |
A | ILE182 |
A | LYS185 |
A | HIS210 |
A | VAL211 |
A | PRO212 |
A | THR217 |
A | ALA238 |
A | SER239 |
A | ARG240 |
A | ASP264 |
A | VAL265 |
A | HIS292 |
A | ILE293 |
A | HOH566 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SER A 451 |
Chain | Residue |
A | HIS344 |
A | GLU345 |
A | ASN346 |
A | ARG347 |
A | VAL350 |
A | HOH500 |
B | ASN364 |
B | ILE365 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD B 450 |
Chain | Residue |
B | ASN108 |
B | VAL112 |
B | GLY158 |
B | TYR159 |
B | GLY160 |
B | HIS161 |
B | ILE162 |
B | TYR180 |
B | ASP181 |
B | ILE182 |
B | LYS185 |
B | HIS210 |
B | VAL211 |
B | PRO212 |
B | THR217 |
B | ALA238 |
B | SER239 |
B | ARG240 |
B | ASP264 |
B | HIS292 |
B | ILE293 |
B | GLY295 |
B | HOH544 |
B | HOH548 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SER B 451 |
Chain | Residue |
A | ILE365 |
A | HOH502 |
B | HIS344 |
B | GLU345 |
B | ASN346 |
B | ARG347 |
B | LEU351 |
B | LEU370 |
A | ASN364 |
site_id | NAA |
Number of Residues | 17 |
Details | NUCLEOTIDE COFACTOR (NAD) BINDING SITE |
Chain | Residue |
A | ASN108 |
A | TYR159 |
A | GLY160 |
A | HIS161 |
A | ILE162 |
A | ASP181 |
A | ILE182 |
A | LYS185 |
A | HIS210 |
A | VAL211 |
A | PRO212 |
A | ALA238 |
A | SER239 |
A | ARG240 |
A | ASP264 |
A | HIS292 |
A | ILE293 |
site_id | NAB |
Number of Residues | 17 |
Details | NUCLEOTIDE COFACTOR (NAD) BINDING SITE |
Chain | Residue |
A | ILE293 |
B | ASN108 |
B | TYR159 |
B | GLY160 |
B | HIS161 |
B | ILE162 |
B | ASP181 |
B | ILE182 |
B | LYS185 |
B | HIS210 |
B | VAL211 |
B | PRO212 |
B | ALA238 |
B | SER239 |
B | ARG240 |
B | ASP264 |
B | ILE293 |
site_id | SEA |
Number of Residues | 6 |
Details | ALLOSTERIC LIGAND (SERINE) SITES |
Chain | Residue |
A | HIS344 |
A | ASN346 |
A | ARG347 |
A | LEU370 |
B | ASN364 |
B | ILE365 |
site_id | SEB |
Number of Residues | 6 |
Details | ALLOSTERIC LIGAND (SERINE) SITES |
Chain | Residue |
B | LEU370 |
A | ASN364 |
A | ILE365 |
B | HIS344 |
B | ASN346 |
B | ARG347 |
Functional Information from PROSITE/UniProt
site_id | PS00065 |
Number of Residues | 28 |
Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGIIGyGHIGtqlgilaeslgmy.VYfYD |
Chain | Residue | Details |
A | LEU154-ASP181 |
site_id | PS00670 |
Number of Residues | 23 |
Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLnmSDVVsLHvPenpsTknMmG |
Chain | Residue | Details |
A | LEU200-GLY222 |
site_id | PS00671 |
Number of Residues | 17 |
Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKpGsLLINaSRGtVVD |
Chain | Residue | Details |
A | MET229-ASP245 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | GLY241 | |
A | PRO270 | |
B | GLY241 | |
B | PRO270 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | ILE293 | |
B | ILE293 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7719856 |
Chain | Residue | Details |
A | ILE162 | |
B | ILE293 | |
A | ILE182 | |
A | SER239 | |
A | VAL265 | |
A | ILE293 | |
B | ILE162 | |
B | ILE182 | |
B | SER239 | |
B | VAL265 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 7719856, 14154, 6848515 |
Chain | Residue | Details |
A | GLU269 | |
A | HIS292 |
site_id | CSA2 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 7719856, 14154, 6848515 |
Chain | Residue | Details |
B | GLU269 | |
B | HIS292 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 785 |
Chain | Residue | Details |
A | PRO270 | electrostatic stabiliser |
A | ILE293 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 785 |
Chain | Residue | Details |
B | PRO270 | electrostatic stabiliser |
B | ILE293 | proton acceptor, proton donor |