6BII
Crystal Structure of Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in complex with NADP and malonate (re-refinement of 5AOW)
Replaces: 5AOWFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
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 | 0016618 | molecular_function | hydroxypyruvate reductase [NAD(P)H] activity |
A | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
A | 0047964 | molecular_function | glyoxylate reductase (NADH) activity |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
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 | 0016618 | molecular_function | hydroxypyruvate reductase [NAD(P)H] activity |
B | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
B | 0047964 | molecular_function | glyoxylate reductase (NADH) activity |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 39 |
Details | binding site for residue NAP A 401 |
Chain | Residue |
A | VAL76 |
A | SER182 |
A | LYS184 |
A | ALA211 |
A | VAL212 |
A | PRO213 |
A | GLU217 |
A | THR218 |
A | VAL239 |
A | ALA240 |
A | ARG241 |
A | THR104 |
A | ASP265 |
A | HIS288 |
A | GLY290 |
A | SER291 |
A | MLI402 |
A | HOH521 |
A | HOH531 |
A | HOH566 |
A | HOH574 |
A | HOH577 |
A | GLY157 |
A | HOH580 |
A | HOH597 |
A | HOH604 |
A | HOH605 |
A | HOH614 |
A | HOH620 |
A | HOH623 |
A | HOH673 |
A | HOH676 |
A | HOH687 |
A | PHE158 |
A | GLY159 |
A | ARG160 |
A | ILE161 |
A | ALA180 |
A | ARG181 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue MLI A 402 |
Chain | Residue |
A | LEU53 |
A | ALA75 |
A | VAL76 |
A | GLY77 |
A | LEU100 |
A | ARG241 |
A | HIS288 |
A | NAP401 |
A | HOH516 |
A | HOH673 |
B | TRP138 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | TYR78 |
A | ASN95 |
A | ARG160 |
A | HOH570 |
A | HOH574 |
A | HOH657 |
A | HOH716 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | HIS30 |
A | GLU31 |
A | HIS32 |
A | HOH690 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | GLN163 |
A | LYS184 |
A | PRO185 |
A | GLU186 |
A | ALA187 |
A | HOH727 |
site_id | AC6 |
Number of Residues | 37 |
Details | binding site for residue NAP B 401 |
Chain | Residue |
B | HOH615 |
B | HOH631 |
B | HOH638 |
B | HOH641 |
B | HOH663 |
B | VAL76 |
B | THR104 |
B | GLY157 |
B | PHE158 |
B | GLY159 |
B | ARG160 |
B | ILE161 |
B | ALA180 |
B | ARG181 |
B | SER182 |
B | LYS184 |
B | ALA211 |
B | VAL212 |
B | PRO213 |
B | THR218 |
B | VAL239 |
B | ALA240 |
B | ARG241 |
B | ASP265 |
B | HIS288 |
B | GLY290 |
B | SER291 |
B | MLI402 |
B | HOH529 |
B | HOH550 |
B | HOH551 |
B | HOH561 |
B | HOH566 |
B | HOH574 |
B | HOH593 |
B | HOH596 |
B | HOH614 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue MLI B 402 |
Chain | Residue |
A | TRP138 |
B | LEU53 |
B | ALA75 |
B | VAL76 |
B | GLY77 |
B | LEU100 |
B | ARG241 |
B | HIS288 |
B | NAP401 |
B | HOH503 |
B | HOH615 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | TYR78 |
B | ASN95 |
B | ARG160 |
B | HOH540 |
B | HOH561 |
B | HOH569 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | LYS184 |
B | PRO185 |
B | GLU186 |
B | ALA187 |
B | HOH553 |
B | HOH685 |
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. MKpTaVLVNvARGkVVD |
Chain | Residue | Details |
A | MET230-ASP246 |