3NDY

The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans

Replaces:  3ICG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
B	0000272	biological_process	polysaccharide catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
C	0000272	biological_process	polysaccharide catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
D	0000272	biological_process	polysaccharide catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005975	biological_process	carbohydrate metabolic process
E	0030246	molecular_function	carbohydrate binding
E	0030247	molecular_function	polysaccharide binding
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0005975	biological_process	carbohydrate metabolic process
F	0030246	molecular_function	carbohydrate binding
F	0030247	molecular_function	polysaccharide binding
G	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
G	0005975	biological_process	carbohydrate metabolic process
G	0030246	molecular_function	carbohydrate binding
G	0030247	molecular_function	polysaccharide binding
H	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
H	0005975	biological_process	carbohydrate metabolic process
H	0030246	molecular_function	carbohydrate binding
H	0030247	molecular_function	polysaccharide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BTB A 1

Chain	Residue
A	HIS107
A	HOH830
A	HIS108
A	TYR229
A	GLU275
A	TRP308
A	GLU319
A	PHE321
A	HOH571
A	HOH592

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BTB B 1

Chain	Residue
B	HIS107
B	HIS108
B	TYR229
B	MET236
B	GLU275
B	TRP308
B	GLU319
B	PHE321
B	HOH629
B	HOH776
B	HOH844

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BTB C 1

Chain	Residue
C	HIS107
C	HIS108
C	GLU152
C	TYR229
C	MET236
C	GLU275
C	TRP308
C	GLU319
C	PHE321
C	HOH539
C	HOH811

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BTB D 1

Chain	Residue
D	HIS107
D	HIS108
D	TYR229
D	MET236
D	GLU275
D	TRP308
D	GLU319
D	PHE321
D	HOH536
D	HOH638

---

Functional Information from PROSITE/UniProt

site_id	PS00659
Number of Residues	10
Details	GLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LIFETMNEPR

Chain	Residue	Details
A	LEU145-ARG154

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1032
Details	Region: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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