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4NUY

Crystal structure of EndoS, an endo-beta-N-acetyl-glucosaminidase from Streptococcus pyogenes

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033925molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
A0042783biological_processsymbiont-mediated evasion of host immune response
A0043655cellular_componenthost extracellular space
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
ALYS786
AASP789
AGLN791
APRO915

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. LDGLDVDvE
ChainResidueDetails
ALEU227-GLU235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsRepeat: {"description":"LRR 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues25
DetailsRepeat: {"description":"LRR 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues23
DetailsRepeat: {"description":"LRR 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues23
DetailsRepeat: {"description":"LRR 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues158
DetailsRegion: {"description":"carbohydrate-binding module (CBM)","evidences":[{"source":"PubMed","id":"24668806","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24753590","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10053","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18182097","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29760474","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EN3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24753590","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29760474","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NUY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NUZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6EN3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24753590","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NUZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Cleavage; by S.pyogenes SpeB","evidences":[{"source":"PubMed","id":"18182097","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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