4JKK

Crystal Structure of Streptococcus agalactiae beta-glucuronidase in space group I222

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004566	molecular_function	beta-glucuronidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0019391	biological_process	glucuronoside catabolic process
A	0030246	molecular_function	carbohydrate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	GLY372
A	GLY372
A	TRP374
A	TRP374

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Functional Information from PROSITE/UniProt

site_id	PS00608
Number of Residues	15
Details	GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPSVVMWVva.NE

Chain	Residue	Details
A	ASP394-GLU408

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site_id	PS00719
Number of Residues	26
Details	GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsFRTSHYPyseeMMrlaDrmGVLVI

Chain	Residue	Details
A	ASN323-ILE348

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Motif: {"description":"N-K motif","evidences":[{"source":"PubMed","id":"26364932","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P05804","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P05804","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P05804","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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