1J0K
Crystal structure of neopullulanase E357Q complex with isopanose
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds | 
| A | 0005509 | molecular_function | calcium ion binding | 
| A | 0005536 | molecular_function | D-glucose binding | 
| A | 0005975 | biological_process | carbohydrate metabolic process | 
| A | 0016787 | molecular_function | hydrolase activity | 
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds | 
| A | 0031216 | molecular_function | neopullulanase activity | 
| A | 0042802 | molecular_function | identical protein binding | 
| A | 0042803 | molecular_function | protein homodimerization activity | 
| A | 0046872 | molecular_function | metal ion binding | 
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds | 
| B | 0005509 | molecular_function | calcium ion binding | 
| B | 0005536 | molecular_function | D-glucose binding | 
| B | 0005975 | biological_process | carbohydrate metabolic process | 
| B | 0016787 | molecular_function | hydrolase activity | 
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds | 
| B | 0031216 | molecular_function | neopullulanase activity | 
| B | 0042802 | molecular_function | identical protein binding | 
| B | 0042803 | molecular_function | protein homodimerization activity | 
| B | 0046872 | molecular_function | metal ion binding | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 2 | 
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000305"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 2 | 
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000305"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 10 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J0H","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 10 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12547200","evidenceCode":"ECO:0000305"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 2 | 
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| A | ASP328 | |
| A | GLN357 | 
| site_id | CSA2 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| B | ASP328 | |
| B | GLN357 | 
| site_id | CSA3 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| A | ASP328 | |
| A | TRP359 | |
| A | GLN357 | |
| A | ASP424 | 
| site_id | CSA4 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| B | ASP328 | |
| B | TRP359 | |
| B | GLN357 | |
| B | ASP424 | 
| site_id | CSA5 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| A | ASP208 | |
| A | ASP269 | 
| site_id | CSA6 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| B | ASP208 | |
| B | ASP269 | 
| site_id | CSA7 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| A | ASP328 | |
| A | GLN357 | |
| A | ASP424 | 
| site_id | CSA8 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1amy | 
| Chain | Residue | Details | 
| B | ASP328 | |
| B | GLN357 | |
| B | ASP424 | 






