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 | 0010466 | biological_process | negative regulation of peptidase 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 | 0010466 | biological_process | negative regulation of peptidase 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 | 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 | 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 | 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) |