2Y8U
A. nidulans chitin deacetylase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0004099 | molecular_function | chitin deacetylase activity |
A | 0005575 | cellular_component | cellular_component |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006032 | biological_process | chitin catabolic process |
A | 0008061 | molecular_function | chitin binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0046872 | molecular_function | metal ion binding |
A | 0071555 | biological_process | cell wall organization |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0004099 | molecular_function | chitin deacetylase activity |
B | 0005575 | cellular_component | cellular_component |
B | 0005576 | cellular_component | extracellular region |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006032 | biological_process | chitin catabolic process |
B | 0008061 | molecular_function | chitin binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0046872 | molecular_function | metal ion binding |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 1238 |
Chain | Residue |
A | ASP47 |
A | ASP48 |
A | HIS97 |
A | HIS101 |
A | TYR138 |
A | HIS196 |
A | CO1239 |
A | HOH2007 |
A | HOH2061 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO A 1239 |
Chain | Residue |
A | ASP48 |
A | HIS97 |
A | HIS101 |
A | PO41238 |
A | HOH2007 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA A 1240 |
Chain | Residue |
A | GLY189 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 1241 |
Chain | Residue |
A | THR34 |
A | NA1244 |
A | HOH2003 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1242 |
Chain | Residue |
A | PHE179 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 1244 |
Chain | Residue |
A | THR34 |
A | PRO125 |
A | NA1241 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 B 1238 |
Chain | Residue |
B | ASP47 |
B | ASP48 |
B | HIS97 |
B | HIS101 |
B | TYR138 |
B | HIS196 |
B | CO1239 |
B | HOH2057 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO B 1239 |
Chain | Residue |
B | ASP48 |
B | HIS97 |
B | HIS101 |
B | PO41238 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 1240 |
Chain | Residue |
B | ARG118 |
B | HOH2029 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01014 |
Chain | Residue | Details |
A | ASP47 | |
B | ASP47 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01014 |
Chain | Residue | Details |
A | HIS196 | |
B | HIS196 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q6DWK3 |
Chain | Residue | Details |
A | ASP47 | |
A | TYR138 | |
B | ASP47 | |
B | TYR138 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01014 |
Chain | Residue | Details |
A | ASP48 | |
A | HIS97 | |
A | HIS101 | |
B | ASP48 | |
B | HIS97 | |
B | HIS101 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: May prevent de-N-acetylated sugar residues from interacting with the active site => ECO:0000303|PubMed:28496100 |
Chain | Residue | Details |
A | LYS164 | |
B | LYS164 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN176 | |
B | ASN176 |