5FL0
Structure of a hydrolase with an inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006517 | biological_process | protein deglycosylation |
| A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006517 | biological_process | protein deglycosylation |
| B | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1716 |
| Chain | Residue |
| B | GLU32 |
| B | GLU61 |
| B | ASP64 |
| B | HOH2019 |
| B | HOH2020 |
| B | HOH2038 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1716 |
| Chain | Residue |
| A | ASN546 |
| A | ASN548 |
| A | HOH2150 |
| A | HOH2153 |
| A | ARG347 |
| A | GLU375 |
| A | HIS376 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1717 |
| Chain | Residue |
| A | TYR137 |
| A | ASP344 |
| A | TYR345 |
| A | ARG347 |
| A | GLN551 |
| A | HOH2152 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1717 |
| Chain | Residue |
| B | ARG347 |
| B | GLU375 |
| B | HIS376 |
| B | ASN546 |
| B | ASN548 |
| B | HOH2163 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1718 |
| Chain | Residue |
| B | PRO303 |
| B | GLN306 |
| B | ARG332 |
| B | SER367 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 71I A 1718 |
| Chain | Residue |
| A | GLY135 |
| A | PHE136 |
| A | TYR137 |
| A | LYS166 |
| A | ASP242 |
| A | ASP243 |
| A | CYS278 |
| A | TYR282 |
| A | MET308 |
| A | TRP309 |
| A | THR310 |
| A | TRP337 |
| A | ASN339 |
| A | ASP344 |
| A | TYR345 |
| A | ASN372 |
| A | HOH2193 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 71I B 1719 |
| Chain | Residue |
| B | GLY135 |
| B | PHE136 |
| B | TYR137 |
| B | LYS166 |
| B | ASP242 |
| B | ASP243 |
| B | CYS278 |
| B | TYR282 |
| B | MET308 |
| B | TRP309 |
| B | THR310 |
| B | VAL314 |
| B | TRP337 |
| B | ASN339 |
| B | ASP344 |
| B | TYR345 |
| B | ASN372 |
| B | HOH2211 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000269|PubMed:16565725 |
| Chain | Residue | Details |
| A | ASP243 | |
| B | ASP243 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16565725 |
| Chain | Residue | Details |
| A | GLY135 | |
| B | ASP242 | |
| B | TYR282 | |
| B | TRP337 | |
| B | ASP344 | |
| B | ASN372 | |
| A | LYS166 | |
| A | ASP242 | |
| A | TYR282 | |
| A | TRP337 | |
| A | ASP344 | |
| A | ASN372 | |
| B | GLY135 | |
| B | LYS166 |
