1V08
Crystal structure of the Zea maze beta-glucosidase-1 in complex with gluco-tetrazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008422 | molecular_function | beta-glucosidase activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009736 | biological_process | cytokinin-activated signaling pathway |
| A | 0015923 | molecular_function | mannosidase activity |
| A | 0015925 | molecular_function | galactosidase activity |
| A | 0015928 | molecular_function | fucosidase activity |
| A | 0016162 | molecular_function | cellulose 1,4-beta-cellobiosidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0097599 | molecular_function | xylanase activity |
| A | 0102726 | molecular_function | DIMBOA glucoside beta-D-glucosidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008422 | molecular_function | beta-glucosidase activity |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009736 | biological_process | cytokinin-activated signaling pathway |
| B | 0015923 | molecular_function | mannosidase activity |
| B | 0015925 | molecular_function | galactosidase activity |
| B | 0015928 | molecular_function | fucosidase activity |
| B | 0016162 | molecular_function | cellulose 1,4-beta-cellobiosidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0097599 | molecular_function | xylanase activity |
| B | 0102726 | molecular_function | DIMBOA glucoside beta-D-glucosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NTZ A1502 |
| Chain | Residue |
| A | GLN38 |
| A | TRP465 |
| A | TYR473 |
| A | NTZ1503 |
| A | HOH2319 |
| A | HIS142 |
| A | ASN190 |
| A | ASP191 |
| A | TYR333 |
| A | TRP378 |
| A | GLU406 |
| A | TRP457 |
| A | GLU464 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NTZ A1503 |
| Chain | Residue |
| A | TRP143 |
| A | THR194 |
| A | TRP378 |
| A | GLU464 |
| A | PHE466 |
| A | NTZ1502 |
| A | HOH2449 |
| A | HOH2450 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NTZ B1502 |
| Chain | Residue |
| B | GLN38 |
| B | HIS142 |
| B | ASN190 |
| B | ASP191 |
| B | TYR333 |
| B | TRP378 |
| B | GLU406 |
| B | TRP457 |
| B | GLU464 |
| B | TRP465 |
| B | TYR473 |
| B | NTZ1503 |
| B | HOH2255 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NTZ B1503 |
| Chain | Residue |
| B | THR194 |
| B | PHE205 |
| B | TRP378 |
| B | GLU464 |
| B | NTZ1502 |
| B | HOH2388 |
| B | HOH2389 |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG |
| Chain | Residue | Details |
| A | ILE402-GLY410 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGaAtSAYQiEgA |
| Chain | Residue | Details |
| A | PHE28-ALA42 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 100 |
| Details | Region: {"description":"Dimerization"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q7XKV4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q7XKV4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106394","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12684498","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1E56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H49","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106394","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1E56","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9SPP9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106394","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12684498","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1E55","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H49","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU406 | |
| A | ASN331 | |
| A | ASP191 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU406 | |
| B | ASN331 | |
| B | ASP191 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU406 | |
| A | ASP191 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU406 | |
| B | ASP191 |
