1RRM
Crystal Structure of Lactaldehyde reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006004 | biological_process | fucose metabolic process |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008912 | molecular_function | lactaldehyde reductase 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 | 0019301 | biological_process | rhamnose catabolic process |
| A | 0019317 | biological_process | fucose catabolic process |
| A | 0042355 | biological_process | L-fucose catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042846 | biological_process | glycol catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052660 | molecular_function | R-lactaldehyde reductase activity |
| A | 0052661 | molecular_function | S-lactaldehyde reductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006004 | biological_process | fucose metabolic process |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0008912 | molecular_function | lactaldehyde reductase 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 | 0019301 | biological_process | rhamnose catabolic process |
| B | 0019317 | biological_process | fucose catabolic process |
| B | 0042355 | biological_process | L-fucose catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042846 | biological_process | glycol catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052660 | molecular_function | R-lactaldehyde reductase activity |
| B | 0052661 | molecular_function | S-lactaldehyde reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 387 |
| Chain | Residue |
| A | ASP196 |
| A | HIS200 |
| A | HIS263 |
| A | HIS277 |
| A | PGO390 |
| A | HOH713 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 387 |
| Chain | Residue |
| B | HIS277 |
| B | PGO390 |
| B | HOH532 |
| B | ASP196 |
| B | HIS200 |
| B | HIS263 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FE2 A 388 |
| Chain | Residue |
| A | CYS362 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FE2 B 388 |
| Chain | Residue |
| B | CYS362 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE APR A 389 |
| Chain | Residue |
| A | ASP39 |
| A | THR41 |
| A | LEU42 |
| A | PRO70 |
| A | ASN71 |
| A | GLY97 |
| A | GLY98 |
| A | SER99 |
| A | PRO100 |
| A | THR140 |
| A | THR141 |
| A | THR144 |
| A | VAL153 |
| A | LYS162 |
| A | MSE181 |
| A | GLY184 |
| A | MSE185 |
| A | LEU189 |
| A | THR193 |
| A | HIS277 |
| A | PGO390 |
| A | HOH415 |
| A | HOH428 |
| A | HOH429 |
| A | HOH441 |
| A | HOH447 |
| A | HOH459 |
| A | HOH468 |
| A | HOH636 |
| A | HOH675 |
| A | HOH713 |
| site_id | AC6 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE APR B 389 |
| Chain | Residue |
| B | ASP39 |
| B | THR41 |
| B | LEU42 |
| B | PRO70 |
| B | ASN71 |
| B | PRO72 |
| B | GLY97 |
| B | GLY98 |
| B | SER99 |
| B | PRO100 |
| B | THR140 |
| B | THR141 |
| B | THR144 |
| B | VAL153 |
| B | LYS162 |
| B | MSE181 |
| B | GLY184 |
| B | MSE185 |
| B | LEU189 |
| B | THR193 |
| B | HIS277 |
| B | PGO390 |
| B | HOH400 |
| B | HOH415 |
| B | HOH428 |
| B | HOH459 |
| B | HOH472 |
| B | HOH474 |
| B | HOH488 |
| B | HOH532 |
| B | HOH651 |
| B | HOH666 |
| B | HOH688 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PGO A 390 |
| Chain | Residue |
| A | ASN151 |
| A | HIS200 |
| A | PHE254 |
| A | HIS263 |
| A | HIS277 |
| A | ZN387 |
| A | APR389 |
| A | HOH402 |
| A | HOH415 |
| A | HOH713 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PGO B 390 |
| Chain | Residue |
| B | ASN151 |
| B | HIS200 |
| B | PHE254 |
| B | HIS263 |
| B | HIS277 |
| B | ZN387 |
| B | APR389 |
| B | HOH415 |
| B | HOH472 |
| B | HOH532 |
Functional Information from PROSITE/UniProt
| site_id | PS00060 |
| Number of Residues | 21 |
| Details | ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. GlVHgmAHpLGAfynTpHGvA |
| Chain | Residue | Details |
| A | GLY260-ALA280 |
| site_id | PS00913 |
| Number of Residues | 29 |
| Details | ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. AFiDadmmdgmPpalkAaTgvDALthaiE |
| Chain | Residue | Details |
| A | ALA175-GLU203 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2BI4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BR4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2BI4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BL4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2BL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BR4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1RRM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BI4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BR4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS267 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| B | HIS267 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS263 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| B | HIS263 |
