1KXT
Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase
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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004556 | molecular_function | alpha-amylase activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016160 | molecular_function | amylase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0031404 | molecular_function | chloride ion binding |
| C | 0043169 | molecular_function | cation binding |
| C | 0046872 | molecular_function | metal ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004556 | molecular_function | alpha-amylase activity |
| E | 0005509 | molecular_function | calcium ion binding |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005615 | cellular_component | extracellular space |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0016052 | biological_process | carbohydrate catabolic process |
| E | 0016160 | molecular_function | amylase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| E | 0031404 | molecular_function | chloride ion binding |
| E | 0043169 | molecular_function | cation binding |
| E | 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 4001 |
| Chain | Residue |
| A | ASN100 |
| A | ARG158 |
| A | ASP167 |
| A | HIS201 |
| A | HOH4221 |
| A | HOH4227 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 4002 |
| Chain | Residue |
| A | ARG195 |
| A | GLU233 |
| A | ARG337 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 4003 |
| Chain | Residue |
| C | ASN100 |
| C | ARG158 |
| C | ASP167 |
| C | HIS201 |
| C | HOH4140 |
| C | HOH4141 |
| C | HOH4275 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 4004 |
| Chain | Residue |
| C | ARG195 |
| C | ASN298 |
| C | ARG337 |
| C | HOH4293 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 4005 |
| Chain | Residue |
| E | ASN100 |
| E | ARG158 |
| E | ASP167 |
| E | HIS201 |
| E | HOH4240 |
| E | HOH4242 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL E 4006 |
| Chain | Residue |
| E | ARG195 |
| E | GLU233 |
| E | ARG337 |
| E | HOH4011 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| 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 | 6 |
| 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 | 3 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| 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 | 3 |
| 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 | 3 |
| 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 | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP300 | |
| C | ASP197 | |
| C | GLU233 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| E | ASP300 | |
| E | ASP197 | |
| E | GLU233 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP197 | |
| A | GLU233 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP197 | |
| C | GLU233 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| E | ASP197 | |
| E | GLU233 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP236 | |
| A | ASP197 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP236 | |
| C | ASP197 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| E | ASP236 | |
| E | ASP197 |
