1VAH
Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016160 | molecular_function | amylase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031404 | molecular_function | chloride ion binding |
A | 0043169 | molecular_function | cation binding |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 498 |
Chain | Residue |
A | ARG195 |
A | ASN298 |
A | ARG337 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 500 |
Chain | Residue |
A | ASN100 |
A | ARG158 |
A | ASP167 |
A | HIS201 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NPO A 701 |
Chain | Residue |
A | ASP300 |
A | HOH587 |
A | TRP59 |
A | GLN63 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8193143","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8681972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8994970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP300 | |
A | ASP197 | |
A | GLU233 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP197 | |
A | GLU233 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP236 | |
A | ASP197 |