2QRK
Crystal Structure of AMP-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003729 | molecular_function | mRNA binding |
A | 0004753 | molecular_function | saccharopine dehydrogenase activity |
A | 0004754 | molecular_function | saccharopine dehydrogenase (NAD+, L-lysine-forming) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005777 | cellular_component | peroxisome |
A | 0006553 | biological_process | lysine metabolic process |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016558 | biological_process | protein import into peroxisome matrix |
A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AMP A 500 |
Chain | Residue |
A | GLY200 |
A | HOH507 |
A | HOH607 |
A | HOH684 |
A | HOH746 |
A | HOH753 |
A | HOH797 |
A | HOH803 |
A | HOH840 |
A | LEU202 |
A | GLY203 |
A | ARG204 |
A | CYS205 |
A | ASP227 |
A | ILE228 |
A | THR231 |
A | ILE250 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687 |
Chain | Residue | Details |
A | LYS77 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687 |
Chain | Residue | Details |
A | HIS96 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1 |
Chain | Residue | Details |
A | ARG18 | |
A | LYS77 | |
A | ARG131 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:3UH1 |
Chain | Residue | Details |
A | GLN101 | |
A | PHE135 | |
A | TYR251 | |
A | SER279 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:3UHA |
Chain | Residue | Details |
A | ARG130 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA |
Chain | Residue | Details |
A | GLY203 | |
A | ASP227 | |
A | THR231 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA |
Chain | Residue | Details |
A | VAL278 | |
A | ILE318 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine; partial => ECO:0000269|Ref.4 |
Chain | Residue | Details |
A | ALA2 |