1XV8
Crystal Structure of Human Salivary Alpha-Amylase Dimer
GO(遺伝子オントロジー)由来の情報
鎖名 | GO(遺伝子オントロジー)id | 名前空間 | 内容 |
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 | 0008152 | biological_process | metabolic process |
A | 0009311 | biological_process | oligosaccharide metabolic 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 |
A | 0070062 | cellular_component | extracellular exosome |
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 | 0008152 | biological_process | metabolic process |
B | 0009311 | biological_process | oligosaccharide metabolic process |
B | 0016160 | molecular_function | amylase activity |
B | 0016787 | molecular_function | hydrolase 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 |
B | 0070062 | cellular_component | extracellular exosome |
PDBデータベースに由来する情報
site_id | AC1 |
残基数 | 5 |
詳細 | BINDING SITE FOR RESIDUE CA A 497 |
鎖名 | 残基 |
A | ASN100 |
A | ARG158 |
A | ASP167 |
A | HIS201 |
A | HOH510 |
site_id | AC2 |
残基数 | 5 |
詳細 | BINDING SITE FOR RESIDUE CA B 497 |
鎖名 | 残基 |
B | HOH513 |
B | ASN100 |
B | ARG158 |
B | ASP167 |
B | HIS201 |
site_id | AC3 |
残基数 | 3 |
詳細 | BINDING SITE FOR RESIDUE CL B 498 |
鎖名 | 残基 |
B | ARG195 |
B | ASN298 |
B | ARG337 |
site_id | AC4 |
残基数 | 3 |
詳細 | BINDING SITE FOR RESIDUE CL A 498 |
鎖名 | 残基 |
A | ARG195 |
A | ASN298 |
A | ARG337 |
SwissProt/UniProtに記載されている蛋白質分子機能情報
site_id | SWS_FT_FI1 |
残基数 | 2 |
詳細 | ACT_SITE: Nucleophile |
鎖名 | 残基 | 詳細 |
A | ASP197 | |
B | ASP197 |
site_id | SWS_FT_FI2 |
残基数 | 2 |
詳細 | ACT_SITE: Proton donor |
鎖名 | 残基 | 詳細 |
A | GLU233 | |
B | GLU233 |
site_id | SWS_FT_FI3 |
残基数 | 14 |
詳細 | BINDING: BINDING => ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD |
鎖名 | 残基 | 詳細 |
A | ASN100 | |
B | ASP167 | |
B | ARG195 | |
B | HIS201 | |
B | ASN298 | |
B | ARG337 | |
A | ARG158 | |
A | ASP167 | |
A | ARG195 | |
A | HIS201 | |
A | ASN298 | |
A | ARG337 | |
B | ASN100 | |
B | ARG158 |
site_id | SWS_FT_FI4 |
残基数 | 2 |
詳細 | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746 |
鎖名 | 残基 | 詳細 |
A | ASP300 | |
B | ASP300 |
site_id | SWS_FT_FI5 |
残基数 | 2 |
詳細 | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P00687 |
鎖名 | 残基 | 詳細 |
A | PCA1 | |
B | PCA1 |
site_id | SWS_FT_FI6 |
残基数 | 4 |
詳細 | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:1710976 |
鎖名 | 残基 | 詳細 |
A | ASN350 | |
A | ASN459 | |
B | ASN350 | |
B | ASN459 |
site_id | SWS_FT_FI7 |
残基数 | 2 |
詳細 | MOD_RES: Deamidated asparagine; partial; alternate => ECO:0000269|PubMed:1710976 |
鎖名 | 残基 | 詳細 |
A | ASN412 | |
B | ASN412 |
site_id | SWS_FT_FI8 |
残基数 | 2 |
詳細 | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:1710976 |
鎖名 | 残基 | 詳細 |
A | ASN412 | |
B | ASN412 |
site_id | SWS_FT_FI9 |
残基数 | 2 |
詳細 | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
鎖名 | 残基 | 詳細 |
A | ASN461 | |
B | ASN461 |