4NUY

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

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	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0033925	molecular_function	mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
A	0042783	biological_process	evasion of host immune response
A	0043655	cellular_component	host extracellular space
A	0046872	molecular_function	metal ion binding
A	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 1001

Chain	Residue
A	LYS786
A	ASP789
A	GLN791
A	PRO915

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Functional Information from PROSITE/UniProt

site_id	PS01095
Number of Residues	9
Details	GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. LDGLDVDvE

Chain	Residue	Details
A	LEU227-GLU235

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000305|PubMed:18182097

Chain	Residue	Details
A	GLU235

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site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:29760474, ECO:0007744|PDB:6EN3

Chain	Residue	Details
A	HIS151
A	TYR402
A	TRP153
A	ARG186
A	ASP237
A	GLN303
A	TYR305
A	GLU349
A	GLU350
A	ASN356

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:24753590, ECO:0000269|PubMed:29760474, ECO:0007744|PDB:4NUY, ECO:0007744|PDB:4NUZ, ECO:0007744|PDB:6EN3

Chain	Residue	Details
A	LYS786
A	ASP789
A	GLN791
A	PRO915

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:24753590, ECO:0007744|PDB:4NUZ

Chain	Residue	Details
A	GLU916

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Cleavage; by S.pyogenes SpeB => ECO:0000269|PubMed:18182097

Chain	Residue	Details
A	LEU445

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