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 | 0051143 | biological_process | propanediol metabolic process |
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 | 0051143 | biological_process | propanediol metabolic process |
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 | 12 |
Details | BINDING: BINDING => ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4 |
Chain | Residue | Details |
A | ASP39 | |
B | LYS162 | |
B | MSE181 | |
B | HIS277 | |
A | GLY98 | |
A | THR140 | |
A | LYS162 | |
A | MSE181 | |
A | HIS277 | |
B | ASP39 | |
B | GLY98 | |
B | THR140 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4 |
Chain | Residue | Details |
A | ASN71 | |
A | ASP342 | |
B | ASN71 | |
B | ASP342 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4 |
Chain | Residue | Details |
A | THR149 | |
B | THR149 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0007744|PDB:1RRM, ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4 |
Chain | Residue | Details |
A | ASP196 | |
A | HIS200 | |
A | HIS263 | |
B | ASP196 | |
B | HIS200 | |
B | HIS263 |