5XG0
Crystal structure of a novel PET hydrolase from Ideonella sakaiensis 201-F6
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0008126 | molecular_function | acetylesterase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042178 | biological_process | xenobiotic catabolic process |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0008126 | molecular_function | acetylesterase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042178 | biological_process | xenobiotic catabolic process |
B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0008126 | molecular_function | acetylesterase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0042178 | biological_process | xenobiotic catabolic process |
C | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535, ECO:0000305|PubMed:29666242 |
Chain | Residue | Details |
A | SER131 | |
B | SER131 | |
C | SER131 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535, ECO:0000305|PubMed:29666242 |
Chain | Residue | Details |
A | ASP177 | |
A | HIS208 | |
B | ASP177 | |
B | HIS208 | |
C | ASP177 | |
C | HIS208 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29235460 |
Chain | Residue | Details |
A | TYR58 | |
A | MET132 | |
B | TYR58 | |
B | MET132 | |
C | TYR58 | |
C | MET132 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29666242 |
Chain | Residue | Details |
A | TRP156 | |
B | TRP156 | |
C | TRP156 |