2DBZ
Crystal Structure of Glyoxylate Reductase (PH0597) from Pyrococcus horikoshii OT3, Complexed with NADP (P61)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| B | TYR78 |
| B | ASN95 |
| B | ARG160 |
| B | HOH530 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | TYR78 |
| A | ASN95 |
| A | ARG160 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | VAL76 |
| B | GLY77 |
| B | ARG241 |
| B | HIS288 |
| B | SER291 |
| B | NAP402 |
| B | LEU53 |
| B | ALA75 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | LEU53 |
| A | ALA75 |
| A | VAL76 |
| A | GLY77 |
| A | LEU100 |
| A | ARG241 |
| A | HIS288 |
| A | SER291 |
| A | NAP401 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP A 401 |
| Chain | Residue |
| A | LYS42 |
| A | VAL76 |
| A | GLY77 |
| A | THR104 |
| A | LEU158 |
| A | GLY159 |
| A | ARG160 |
| A | ILE161 |
| A | SER180 |
| A | ARG181 |
| A | THR182 |
| A | ALA211 |
| A | PRO213 |
| A | GLU217 |
| A | THR218 |
| A | ILE239 |
| A | ALA240 |
| A | ARG241 |
| A | ASP265 |
| A | HIS288 |
| A | GLY290 |
| A | SER291 |
| A | SO4504 |
| A | HOH512 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP B 402 |
| Chain | Residue |
| B | LYS42 |
| B | VAL76 |
| B | GLY77 |
| B | THR104 |
| B | GLY157 |
| B | LEU158 |
| B | GLY159 |
| B | ARG160 |
| B | ILE161 |
| B | SER180 |
| B | ARG181 |
| B | THR182 |
| B | ALA211 |
| B | VAL212 |
| B | PRO213 |
| B | GLU217 |
| B | THR218 |
| B | ILE239 |
| B | ALA240 |
| B | ARG241 |
| B | ASP265 |
| B | HIS288 |
| B | GLY290 |
| B | SER291 |
| B | SO4503 |
| B | HOH510 |
| B | HOH530 |
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. IGIIGlGRIGqaiakrakgfnmr.ILyYS |
| Chain | Residue | Details |
| A | ILE153-SER180 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKkTaILINiARGkVVD |
| Chain | Residue | Details |
| A | MET230-ASP246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of glyoxylate reductase (ph0597) from Pyrococcus horikoshii OT3, complexed with nadp (i41).","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| A | LYS243 | |
| A | ASP265 | |
| A | ARG241 | |
| A | GLU270 | |
| A | HIS288 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| B | LYS243 | |
| B | ASP265 | |
| B | ARG241 | |
| B | GLU270 | |
| B | HIS288 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| A | GLU270 | |
| A | HIS288 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| B | GLU270 | |
| B | HIS288 |
