6MDS
Crystal structure of Streptococcus pyogenes endo-beta-N-acetylglucosaminidase (EndoS2) with complex biantennary glycan
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0033925 | molecular_function | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity |
A | 0042783 | biological_process | symbiont-mediated evasion of host immune response |
A | 0043655 | cellular_component | host extracellular space |
A | 0046872 | molecular_function | metal ion binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0033925 | molecular_function | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity |
B | 0042783 | biological_process | symbiont-mediated evasion of host immune response |
B | 0043655 | cellular_component | host extracellular space |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS01095 |
Number of Residues | 9 |
Details | GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. VDGLDIDiE |
Chain | Residue | Details |
A | VAL178-GLU186 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000305|PubMed:23865566 |
Chain | Residue | Details |
A | GLU186 | |
B | GLU186 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6MDS, ECO:0007744|PDB:6MDV |
Chain | Residue | Details |
A | ARG72 | |
B | ARG72 | |
B | TRP74 | |
B | ASP108 | |
B | HIS109 | |
B | TYR252 | |
B | GLU288 | |
B | GLU289 | |
B | ASN295 | |
B | TYR339 | |
A | TRP74 | |
A | ASP108 | |
A | HIS109 | |
A | TYR252 | |
A | GLU288 | |
A | GLU289 | |
A | ASN295 | |
A | TYR339 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6MDV |
Chain | Residue | Details |
A | HIS88 | |
B | HIS88 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6MDS |
Chain | Residue | Details |
A | HIS107 | |
A | ASP184 | |
A | GLN250 | |
B | HIS107 | |
B | ASP184 | |
B | GLN250 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30937380, ECO:0007744|PDB:6E58, ECO:0007744|PDB:6MDS, ECO:0007744|PDB:6MDV |
Chain | Residue | Details |
A | LYS699 | |
B | ASP707 | |
B | THR824 | |
B | GLU825 | |
A | ASP702 | |
A | GLU704 | |
A | ASP707 | |
A | THR824 | |
A | GLU825 | |
B | LYS699 | |
B | ASP702 | |
B | GLU704 |