1J0H
Crystal structure of Bacillus stearothermophilus neopullulanase
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 | glucose binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008152 | biological_process | 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 | glucose binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008152 | biological_process | 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 PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 600 |
| Chain | Residue |
| A | THR227 |
| A | ARG231 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 601 |
| Chain | Residue |
| A | ASN147 |
| A | ASN149 |
| A | SER153 |
| A | GLY172 |
| A | ASP174 |
| A | HOH1427 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 602 |
| Chain | Residue |
| B | ASN149 |
| B | SER153 |
| B | GLY172 |
| B | ASP174 |
| B | HOH1415 |
| B | ASN147 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:12547200 |
| Chain | Residue | Details |
| A | ASP328 | |
| B | ASP328 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:12547200 |
| Chain | Residue | Details |
| A | GLU357 | |
| B | GLU357 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12547200, ECO:0007744|PDB:1J0H |
| Chain | Residue | Details |
| B | ASN149 | |
| B | SER153 | |
| B | GLY172 | |
| B | ASP174 | |
| A | ASN147 | |
| A | ASN149 | |
| A | SER153 | |
| A | GLY172 | |
| A | ASP174 | |
| B | ASN147 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12547200 |
| Chain | Residue | Details |
| A | ARG472 | |
| B | HIS247 | |
| B | ARG326 | |
| B | HIS423 | |
| B | ASP468 | |
| B | ARG472 | |
| A | HIS247 | |
| A | ARG326 | |
| A | HIS423 | |
| A | ASP468 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP424 | |
| B | ASP424 |
