4E5K
Thermostable phosphite dehydrogenase in complex with NAD and sulfite
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0008465 | molecular_function | hydroxypyruvate reductase (NADH) activity |
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 | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
A | 0050609 | molecular_function | phosphonate dehydrogenase activity |
A | 0051287 | molecular_function | NAD binding |
B | 0005829 | cellular_component | cytosol |
B | 0008465 | molecular_function | hydroxypyruvate reductase (NADH) activity |
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 | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
B | 0050609 | molecular_function | phosphonate dehydrogenase activity |
B | 0051287 | molecular_function | NAD binding |
C | 0005829 | cellular_component | cytosol |
C | 0008465 | molecular_function | hydroxypyruvate reductase (NADH) activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
C | 0050609 | molecular_function | phosphonate dehydrogenase activity |
C | 0051287 | molecular_function | NAD binding |
D | 0005829 | cellular_component | cytosol |
D | 0008465 | molecular_function | hydroxypyruvate reductase (NADH) activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
D | 0050609 | molecular_function | phosphonate dehydrogenase activity |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD A 401 |
Chain | Residue |
A | LYS76 |
A | ALA176 |
A | ALA207 |
A | LEU208 |
A | PRO209 |
A | PRO235 |
A | CYS236 |
A | ARG237 |
A | ASP261 |
A | HIS292 |
A | GLY294 |
A | GLY77 |
A | SO3402 |
A | HOH501 |
A | HOH509 |
A | HOH514 |
A | HOH560 |
A | HOH578 |
A | HOH611 |
A | HOH637 |
A | THR104 |
A | GLY152 |
A | GLY154 |
A | ALA155 |
A | ILE156 |
A | HIS174 |
A | GLU175 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO3 A 402 |
Chain | Residue |
A | MET53 |
A | LEU75 |
A | LYS76 |
A | GLY77 |
A | LEU100 |
A | ARG237 |
A | HIS292 |
A | NAD401 |
A | HOH637 |
site_id | AC3 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAD B 401 |
Chain | Residue |
B | LYS76 |
B | GLY77 |
B | THR104 |
B | GLY152 |
B | GLY154 |
B | ALA155 |
B | ILE156 |
B | HIS174 |
B | GLU175 |
B | ALA176 |
B | ALA207 |
B | LEU208 |
B | PRO209 |
B | PRO235 |
B | CYS236 |
B | ARG237 |
B | ASP261 |
B | VAL262 |
B | HIS292 |
B | GLY294 |
B | SO3402 |
B | HOH504 |
B | HOH528 |
B | HOH537 |
B | HOH559 |
B | HOH574 |
B | HOH600 |
B | HOH624 |
B | HOH647 |
B | HOH668 |
B | HOH676 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO3 B 402 |
Chain | Residue |
B | MET53 |
B | LEU75 |
B | LYS76 |
B | GLY77 |
B | ARG237 |
B | HIS292 |
B | NAD401 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD C 401 |
Chain | Residue |
C | HOH578 |
C | LYS76 |
C | GLY77 |
C | THR104 |
C | GLY152 |
C | GLY154 |
C | ALA155 |
C | ILE156 |
C | HIS174 |
C | GLU175 |
C | ALA176 |
C | ALA207 |
C | LEU208 |
C | PRO209 |
C | LEU217 |
C | PRO235 |
C | CYS236 |
C | ARG237 |
C | ASP261 |
C | HIS292 |
C | GLY294 |
C | SO3402 |
C | HOH515 |
C | HOH524 |
C | HOH534 |
C | HOH552 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO3 C 402 |
Chain | Residue |
C | MET53 |
C | LEU75 |
C | LYS76 |
C | GLY77 |
C | ARG237 |
C | HIS292 |
C | NAD401 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO3 D 401 |
Chain | Residue |
D | MET53 |
D | LEU75 |
D | LYS76 |
D | GLY77 |
D | LEU100 |
D | ARG237 |
D | HIS292 |
site_id | AC8 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD D 402 |
Chain | Residue |
D | LYS76 |
D | THR104 |
D | GLY152 |
D | GLY154 |
D | ALA155 |
D | ILE156 |
D | HIS174 |
D | GLU175 |
D | ALA176 |
D | ALA207 |
D | LEU208 |
D | PRO209 |
D | LEU217 |
D | PRO235 |
D | CYS236 |
D | ARG237 |
D | ASP261 |
D | HIS292 |
D | GLY294 |
D | HOH524 |
D | HOH532 |
Functional Information from PROSITE/UniProt
site_id | PS00671 |
Number of Residues | 17 |
Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. VRpGaLLVNpCRGsVVD |
Chain | Residue | Details |
A | VAL226-ASP242 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | ARG237 | |
A | GLU266 | |
B | ARG237 | |
B | GLU266 | |
C | ARG237 | |
C | GLU266 | |
D | ARG237 | |
D | GLU266 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | HIS292 | |
B | HIS292 | |
C | HIS292 | |
D | HIS292 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ALA155 | |
B | HIS292 | |
C | ALA155 | |
C | GLU175 | |
C | PRO235 | |
C | ASP261 | |
C | HIS292 | |
D | ALA155 | |
D | GLU175 | |
D | PRO235 | |
D | ASP261 | |
A | GLU175 | |
D | HIS292 | |
A | PRO235 | |
A | ASP261 | |
A | HIS292 | |
B | ALA155 | |
B | GLU175 | |
B | PRO235 | |
B | ASP261 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 984 |
Chain | Residue | Details |
B | MET53 | electrostatic stabiliser |
B | ARG237 | electrostatic stabiliser |
B | HIS292 | proton acceptor, proton donor |