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 |
