3VXD

Crystal structure of unsaturated glucuronyl hydrolase mutant D115N from Streptcoccus agalactiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0005975	biological_process	carbohydrate metabolic process
A	0009405	biological_process	obsolete pathogenesis
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0052757	molecular_function	chondroitin hydrolase activity
A	0102212	molecular_function	unsaturated chondroitin disaccharide hydrolase activity
B	0000272	biological_process	polysaccharide catabolic process
B	0005975	biological_process	carbohydrate metabolic process
B	0009405	biological_process	obsolete pathogenesis
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0052757	molecular_function	chondroitin hydrolase activity
B	0102212	molecular_function	unsaturated chondroitin disaccharide hydrolase activity
C	0000272	biological_process	polysaccharide catabolic process
C	0005975	biological_process	carbohydrate metabolic process
C	0009405	biological_process	obsolete pathogenesis
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0052757	molecular_function	chondroitin hydrolase activity
C	0102212	molecular_function	unsaturated chondroitin disaccharide hydrolase activity
D	0000272	biological_process	polysaccharide catabolic process
D	0005975	biological_process	carbohydrate metabolic process
D	0009405	biological_process	obsolete pathogenesis
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0052757	molecular_function	chondroitin hydrolase activity
D	0102212	molecular_function	unsaturated chondroitin disaccharide hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	TYR290
A	GLY298
A	GLY300
A	HOH541

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 401

Chain	Residue
B	TYR290
B	GLY298
B	GLY300
B	HOH558

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 401

Chain	Residue
C	ARG356
C	ASN59

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 402

Chain	Residue
C	TYR290
C	GLY298
C	SER299
C	GLY300
C	HOH612
C	HOH628

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 401

Chain	Residue
D	TYR290
D	GLY298
D	SER299
D	GLY300
D	HOH617

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 402

Chain	Residue
D	ARG17
D	GLU285
D	LYS287

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19416976","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"19416976","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

---