1JIB
Complex of Alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with Maltotetraose Based on a Crystal Soaked with Maltohexaose.
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031216 | molecular_function | neopullulanase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0031216 | molecular_function | neopullulanase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P38940 |
Chain | Residue | Details |
A | ASN325 | |
B | ASN325 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940 |
Chain | Residue | Details |
A | GLU354 | |
B | GLU354 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2 |
Chain | Residue | Details |
A | ASN143 | |
B | ASP149 | |
B | GLY169 | |
B | ASP171 | |
A | ASP145 | |
A | ASN148 | |
A | ASP149 | |
A | GLY169 | |
A | ASP171 | |
B | ASN143 | |
B | ASP145 | |
B | ASN148 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P38940 |
Chain | Residue | Details |
A | HIS244 | |
B | ARG469 | |
A | ARG323 | |
A | HIS420 | |
A | ASP465 | |
A | ARG469 | |
B | HIS244 | |
B | ARG323 | |
B | HIS420 | |
B | ASP465 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | ASP421 | |
B | ASP421 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | TRP356 | |
A | ASN325 | |
A | ASP421 | |
A | GLU354 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
B | TRP356 | |
B | ASN325 | |
B | ASP421 | |
B | GLU354 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP421 | |
A | ASN325 | |
A | GLU354 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
B | ASP421 | |
B | ASN325 | |
B | GLU354 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASN325 | |
A | GLU354 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
B | ASN325 | |
B | GLU354 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 433 |
Chain | Residue | Details |
A | ASN325 | covalent catalysis |
A | GLU354 | proton shuttle (general acid/base) |
A | ASP421 | transition state stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 433 |
Chain | Residue | Details |
B | ASN325 | covalent catalysis |
B | GLU354 | proton shuttle (general acid/base) |
B | ASP421 | transition state stabiliser |