2BGM
X-Ray structure of ternary-Secoisolariciresinol Dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0009807 | biological_process | lignan biosynthetic process |
| 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 | 0051289 | biological_process | protein homotetramerization |
| A | 0120529 | molecular_function | secoisolariciresinol dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAJ A1300 |
| Chain | Residue |
| A | GLY23 |
| A | ASN99 |
| A | VAL100 |
| A | GLY101 |
| A | THR151 |
| A | ALA152 |
| A | SER153 |
| A | TYR167 |
| A | LYS171 |
| A | PRO197 |
| A | TYR198 |
| A | GLY26 |
| A | ILE199 |
| A | VAL200 |
| A | HOH2007 |
| A | HOH2123 |
| A | HOH2124 |
| A | MAX6001 |
| A | GLY27 |
| A | ILE28 |
| A | ASP47 |
| A | ILE48 |
| A | CYS71 |
| A | ASP72 |
| A | VAL73 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE MAX A6001 |
| Chain | Residue |
| A | LEU103 |
| A | SER104 |
| A | ILE154 |
| A | GLY162 |
| A | VAL163 |
| A | SER164 |
| A | TYR167 |
| A | PRO197 |
| A | TYR198 |
| A | ILE199 |
| A | NAJ1300 |
| A | HOH2067 |
| A | HOH2125 |
| A | HOH2126 |
| A | HOH2127 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. IssftagegvShvYTATKHAVlGLTtSLC |
| Chain | Residue | Details |
| A | ILE154-CYS182 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15653677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16493463","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BGL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BGM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15653677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BGL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BGM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2BGL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BGM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR167 | |
| A | LYS171 | |
| A | SER153 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR167 | |
| A | ASN125 | |
| A | LYS171 | |
| A | SER153 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR167 | |
| A | LYS171 |
