1AVA
AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005983 | biological_process | starch catabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004556 | molecular_function | alpha-amylase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005983 | biological_process | starch catabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0043169 | molecular_function | cation binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004866 | molecular_function | endopeptidase inhibitor activity |
| C | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| C | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| D | 0004866 | molecular_function | endopeptidase inhibitor activity |
| D | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| D | 0015066 | molecular_function | alpha-amylase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 500 |
| Chain | Residue |
| A | ASP148 |
| A | GLY183 |
| A | HOH601 |
| A | ASN91 |
| A | ASP138 |
| A | ALA141 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | GLU108 |
| A | THR111 |
| A | ASP113 |
| A | ASP117 |
| A | HOH575 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 502 |
| Chain | Residue |
| A | ASP127 |
| A | ASP142 |
| A | PHE143 |
| A | ALA146 |
| A | ASP148 |
| A | HOH584 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | HOH597 |
| A | HOH611 |
| A | HOH612 |
| A | HOH644 |
| A | HOH741 |
| A | HOH795 |
| C | HOH185 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 500 |
| Chain | Residue |
| B | ASN91 |
| B | ASP138 |
| B | ALA141 |
| B | ASP148 |
| B | GLY183 |
| B | HOH582 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 501 |
| Chain | Residue |
| B | GLU108 |
| B | THR111 |
| B | ASP113 |
| B | ASP117 |
| B | HOH664 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | ASP127 |
| B | ASP142 |
| B | PHE143 |
| B | ALA146 |
| B | ASP148 |
| B | HOH581 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | HOH572 |
| B | HOH573 |
| B | HOH576 |
| B | HOH616 |
| B | HOH617 |
| B | HOH652 |
| D | HOH336 |
| site_id | ACA |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| A | GLU204 |
| A | ASP289 |
| A | ASP179 |
| site_id | ACB |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| B | GLU204 |
| B | ASP289 |
| B | ASP179 |
Functional Information from PROSITE/UniProt
| site_id | PS00283 |
| Number of Residues | 17 |
| Details | SOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. VhDTDGHeLrADanYyV |
| Chain | Residue | Details |
| C | VAL6-VAL22 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | SITE: Reactive bond => ECO:0000250 |
| Chain | Residue | Details |
| C | VAL67 | |
| D | VAL67 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:9571044 |
| Chain | Residue | Details |
| A | GLU204 | |
| B | GLU204 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:9571044 |
| Chain | Residue | Details |
| A | TYR51 | |
| B | ARG177 | |
| B | TRP206 | |
| B | SER208 | |
| B | GLN226 | |
| B | ASP233 | |
| B | GLY275 | |
| B | HIS288 | |
| A | ARG177 | |
| A | TRP206 | |
| A | SER208 | |
| A | GLN226 | |
| A | ASP233 | |
| A | GLY275 | |
| A | HIS288 | |
| B | TYR51 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 26 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA |
| Chain | Residue | Details |
| A | ASN91 | |
| A | PHE143 | |
| A | ALA146 | |
| A | ASP148 | |
| A | GLY183 | |
| B | ASN91 | |
| B | GLU108 | |
| B | THR111 | |
| B | ASP113 | |
| B | ASP117 | |
| B | ASP127 | |
| A | GLU108 | |
| B | ASP138 | |
| B | ALA141 | |
| B | ASP142 | |
| B | PHE143 | |
| B | ALA146 | |
| B | ASP148 | |
| B | GLY183 | |
| A | THR111 | |
| A | ASP113 | |
| A | ASP117 | |
| A | ASP127 | |
| A | ASP138 | |
| A | ALA141 | |
| A | ASP142 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00693 |
| Chain | Residue | Details |
| A | LYS269 | |
| B | TRP400 | |
| A | GLN294 | |
| A | LYS373 | |
| A | VAL390 | |
| A | TRP400 | |
| B | LYS269 | |
| B | GLN294 | |
| B | LYS373 | |
| B | VAL390 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:9571044 |
| Chain | Residue | Details |
| A | ASP289 | |
| B | ASP289 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | GLU204 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP179 | |
| B | GLU204 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | ASP233 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP179 | |
| B | ASP233 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | GLU204 | |
| A | TRP206 | |
| A | ASP289 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP179 | |
| B | GLU204 | |
| B | TRP206 | |
| B | ASP289 |
| site_id | CSA7 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | GLU204 | |
| A | ASP179 | |
| A | ARG177 | |
| A | ASP289 | |
| A | HIS288 |
| site_id | CSA8 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | GLU204 | |
| B | ASP179 | |
| B | ARG177 | |
| B | ASP289 | |
| B | HIS288 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | GLU204 | |
| A | ASP179 | |
| A | HIS92 | |
| A | ASP289 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | GLU204 | |
| B | ASP179 | |
| B | HIS92 | |
| B | ASP289 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | GLU204 | |
| A | ASP289 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP179 | |
| B | GLU204 | |
| B | ASP289 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | ASP289 | |
| A | GLU227 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP179 | |
| B | ASP289 | |
| B | GLU227 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 397 |
| Chain | Residue | Details |
| A | ASP179 | covalent catalysis |
| A | GLU204 | hydrogen radical acceptor, proton shuttle (general acid/base) |
| A | ASP289 | electrostatic stabiliser, hydrogen radical acceptor, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 397 |
| Chain | Residue | Details |
| B | ASP179 | covalent catalysis |
| B | GLU204 | hydrogen radical acceptor, proton shuttle (general acid/base) |
| B | ASP289 | electrostatic stabiliser, hydrogen radical acceptor, proton shuttle (general acid/base) |
