1JI1
Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005576 | cellular_component | extracellular region |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2001 |
| Chain | Residue |
| A | ALA2 |
| A | ASP4 |
| A | ASN6 |
| A | ASP42 |
| A | ASP96 |
| A | HOH2487 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 2002 |
| Chain | Residue |
| A | ASP151 |
| A | GLY187 |
| A | ASP189 |
| A | HOH2145 |
| A | ASN145 |
| A | ASP147 |
| A | ASN150 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2003 |
| Chain | Residue |
| A | ASP276 |
| A | ASN279 |
| A | PHE281 |
| A | SER283 |
| A | GLU288 |
| A | HOH2478 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2004 |
| Chain | Residue |
| B | ALA2 |
| B | ASP4 |
| B | ASN6 |
| B | ASP42 |
| B | ASP96 |
| B | HOH2098 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 2005 |
| Chain | Residue |
| B | ASN145 |
| B | ASP147 |
| B | ASN150 |
| B | ASP151 |
| B | GLY187 |
| B | ASP189 |
| B | HOH2526 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2006 |
| Chain | Residue |
| B | ASP276 |
| B | ASN279 |
| B | PHE281 |
| B | SER283 |
| B | GLU288 |
| B | HOH2156 |
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 | ASP356 | |
| B | ASP356 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| A | GLU396 | |
| B | GLU396 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1 |
| Chain | Residue | Details |
| A | ALA2 | |
| A | GLY187 | |
| A | ASP189 | |
| A | ASP276 | |
| A | ASN280 | |
| A | PHE281 | |
| A | SER283 | |
| A | GLU288 | |
| B | ALA2 | |
| B | ASP4 | |
| B | ASN6 | |
| A | ASP4 | |
| B | ASP42 | |
| B | ASP96 | |
| B | ASN145 | |
| B | ASP147 | |
| B | ASN150 | |
| B | ASP151 | |
| B | GLY187 | |
| B | ASP189 | |
| B | ASP276 | |
| B | ASN280 | |
| A | ASN6 | |
| B | PHE281 | |
| B | SER283 | |
| B | GLU288 | |
| A | ASP42 | |
| A | ASP96 | |
| A | ASN145 | |
| A | ASP147 | |
| A | ASN150 | |
| A | ASP151 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| A | HIS267 | |
| B | ARG520 | |
| A | ARG354 | |
| A | HIS471 | |
| A | ASP516 | |
| A | ARG520 | |
| B | HIS267 | |
| B | ARG354 | |
| B | HIS471 | |
| B | ASP516 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP472 | |
| B | ASP472 |
