6JE8
crystal structure of a beta-N-acetylhexosaminidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030203 | biological_process | glycosaminoglycan metabolic process |
| A | 0032428 | molecular_function | beta-N-acetylgalactosaminidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052781 | biological_process | chitobiose catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | CYS227 |
| A | CYS247 |
| A | CYS288 |
| A | CYS291 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GOL503 |
| A | HOH672 |
| A | HOH725 |
| A | HIS214 |
| A | ASP278 |
| A | TRP345 |
| A | TYR373 |
| A | TRP421 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TYR373 |
| A | ASP375 |
| A | TRP387 |
| A | TRP421 |
| A | GLU423 |
| A | GOL502 |
| A | HOH683 |
| A | HOH725 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | GLY161 |
| A | TYR162 |
| A | GLU224 |
| A | HOH601 |
| A | HOH621 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | TYR371 |
| A | ASP398 |
| A | ASP400 |
| A | PHE403 |
| A | HOH729 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | ASN429 |
| A | TYR475 |
| A | ASP476 |
| A | ASN483 |
| A | HOH742 |
| A | HOH963 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 507 |
| Chain | Residue |
| A | ARG87 |
| A | ARG90 |
| A | LYS255 |
| A | ARG472 |
| A | HOH615 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"30846208","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6JE8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JEB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"30846208","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6JEB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30846208","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6JEA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30846208","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6JE8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JEB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
