2IX9
Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0005576 | cellular_component | extracellular region |
A | 0006629 | biological_process | lipid metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0030245 | biological_process | cellulose catabolic process |
A | 0030248 | molecular_function | cellulose binding |
A | 0030600 | molecular_function | feruloyl esterase activity |
A | 0044347 | biological_process | cell wall polysaccharide catabolic process |
A | 0045490 | biological_process | pectin catabolic process |
A | 0045493 | biological_process | xylan catabolic process |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0005576 | cellular_component | extracellular region |
B | 0006629 | biological_process | lipid metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016998 | biological_process | cell wall macromolecule catabolic process |
B | 0030245 | biological_process | cellulose catabolic process |
B | 0030248 | molecular_function | cellulose binding |
B | 0030600 | molecular_function | feruloyl esterase activity |
B | 0044347 | biological_process | cell wall polysaccharide catabolic process |
B | 0045490 | biological_process | pectin catabolic process |
B | 0045493 | biological_process | xylan catabolic process |
B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A1267 |
Chain | Residue |
A | ARG162 |
A | ALA207 |
A | HIS208 |
A | HOH2281 |
A | HOH2282 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B1265 |
Chain | Residue |
B | ARG162 |
B | ALA207 |
B | HIS208 |
B | HOH2243 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CXS A1261 |
Chain | Residue |
A | TYR25 |
A | THR68 |
A | SER133 |
A | HIS247 |
A | SER255 |
A | GLY256 |
A | EDO1265 |
A | HOH2271 |
A | HOH2272 |
A | HOH2273 |
A | HOH2274 |
B | ASP71 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A1262 |
Chain | Residue |
A | ASP77 |
A | TYR80 |
A | HIS97 |
A | TYR100 |
A | LEU199 |
A | EDO1264 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO A1263 |
Chain | Residue |
A | GLU160 |
A | SER163 |
A | GLY164 |
A | PHE168 |
A | ALA169 |
A | MET172 |
A | TYR186 |
A | ALA207 |
A | GLY209 |
A | HOH2276 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A1264 |
Chain | Residue |
A | ASP77 |
A | TYR100 |
A | SER133 |
A | EDO1262 |
A | HOH2277 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A1265 |
Chain | Residue |
A | THR248 |
A | THR254 |
A | SER255 |
A | CXS1261 |
A | HOH2266 |
A | HOH2278 |
B | GLN45 |
B | ASP71 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A1266 |
Chain | Residue |
A | SER7 |
A | GLU8 |
A | ASP9 |
A | HOH2279 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CXS B1261 |
Chain | Residue |
A | ASP71 |
A | LEU74 |
A | HOH2102 |
B | TYR25 |
B | THR68 |
B | HIS247 |
B | SER255 |
B | GLY256 |
B | HOH2240 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B1262 |
Chain | Residue |
B | ASP77 |
B | TYR80 |
B | HIS97 |
B | TYR100 |
B | EDO1264 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B1263 |
Chain | Residue |
B | GLU160 |
B | SER163 |
B | GLY164 |
B | PHE168 |
B | TYR186 |
B | ALA207 |
B | GLY209 |
B | HOH2241 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B1264 |
Chain | Residue |
B | LEU74 |
B | ASP77 |
B | VAL243 |
B | EDO1262 |
B | HOH2242 |
Functional Information from PROSITE/UniProt
site_id | PS00120 |
Number of Residues | 10 |
Details | LIPASE_SER Lipases, serine active site. LTVTGHSLGA |
Chain | Residue | Details |
A | LEU127-ALA136 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:15081808 |
Chain | Residue | Details |
A | SER133 | |
B | SER133 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:15103133 |
Chain | Residue | Details |
A | ASP194 | |
A | HIS247 | |
B | ASP194 | |
B | HIS247 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16128806 |
Chain | Residue | Details |
A | ASP77 | |
A | TYR80 | |
A | HIS247 | |
B | ASP77 | |
B | TYR80 | |
B | HIS247 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17027758 |
Chain | Residue | Details |
A | ASN79 | |
B | ASN79 |