1KXQ
Camelid VHH Domain 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 | 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004556 | molecular_function | alpha-amylase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016160 | molecular_function | amylase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031404 | molecular_function | chloride ion binding |
| B | 0043169 | molecular_function | cation binding |
| B | 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 | 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 |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004556 | molecular_function | alpha-amylase activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016160 | molecular_function | amylase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0031404 | molecular_function | chloride ion binding |
| D | 0043169 | molecular_function | cation binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 4001 |
| Chain | Residue |
| A | ASN100 |
| A | ARG158 |
| A | ASP167 |
| A | HIS201 |
| A | HOH4014 |
| A | HOH4094 |
| A | HOH4125 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 4002 |
| Chain | Residue |
| A | ARG337 |
| A | ARG195 |
| A | ASN298 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 4003 |
| Chain | Residue |
| B | ASN100 |
| B | ARG158 |
| B | ASP167 |
| B | HIS201 |
| B | HOH4012 |
| B | HOH4030 |
| B | HOH4307 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 4004 |
| Chain | Residue |
| B | ARG195 |
| B | ASN298 |
| B | ARG337 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 4005 |
| Chain | Residue |
| C | ASN100 |
| C | ARG158 |
| C | ASP167 |
| C | HIS201 |
| C | HOH4022 |
| C | HOH4047 |
| C | HOH4060 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 4006 |
| Chain | Residue |
| C | ARG195 |
| C | ASN298 |
| C | ARG337 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA D 4007 |
| Chain | Residue |
| D | ASN100 |
| D | ARG158 |
| D | ASP167 |
| D | HIS201 |
| D | HOH4016 |
| D | HOH4038 |
| D | HOH4041 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 4008 |
| Chain | Residue |
| D | ARG195 |
| D | ASN298 |
| D | ARG337 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ASP212 | |
| B | ASP212 | |
| C | ASP212 | |
| D | ASP212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | PHE248 | |
| B | PHE248 | |
| C | PHE248 | |
| D | PHE248 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631 |
| Chain | Residue | Details |
| A | CYS115 | |
| C | ASP173 | |
| C | TYR182 | |
| C | ASN216 | |
| D | CYS115 | |
| D | ASP173 | |
| D | TYR182 | |
| D | ASN216 | |
| A | ASP173 | |
| A | TYR182 | |
| A | ASN216 | |
| B | CYS115 | |
| B | ASP173 | |
| B | TYR182 | |
| B | ASN216 | |
| C | CYS115 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631 |
| Chain | Residue | Details |
| A | VAL210 | |
| A | GLU352 | |
| B | VAL210 | |
| B | GLU352 | |
| C | VAL210 | |
| C | GLU352 | |
| D | VAL210 | |
| D | GLU352 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | LEU313 | |
| B | LEU313 | |
| C | LEU313 | |
| D | LEU313 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746 |
| Chain | Residue | Details |
| A | PHE315 | |
| B | PHE315 | |
| C | PHE315 | |
| D | PHE315 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P04746 |
| Chain | Residue | Details |
| A | LEU16 | |
| B | LEU16 | |
| C | LEU16 | |
| D | LEU16 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| A | ILE427 | |
| B | ILE427 | |
| C | ILE427 | |
| D | ILE427 |
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 | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP236 | |
| B | ASP197 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP236 | |
| C | ASP197 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP236 | |
| D | ASP197 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP300 | |
| B | ASP197 | |
| B | GLU233 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP300 | |
| C | ASP197 | |
| C | GLU233 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP300 | |
| D | ASP197 | |
| D | GLU233 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP197 | |
| A | GLU233 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP197 | |
| B | GLU233 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP197 | |
| C | GLU233 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP197 | |
| D | GLU233 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP236 | |
| A | ASP197 |
