2ZUN

Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii

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
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046872	molecular_function	metal ion binding
B	0000272	biological_process	polysaccharide catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0046872	molecular_function	metal ion binding
C	0000272	biological_process	polysaccharide catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE194-HIS203

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1bqc

Chain	Residue	Details
A	GLU342
A	GLU201
A	ASN200
A	HIS297
A	TYR299

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1bqc

Chain	Residue	Details
B	GLU342
B	GLU201
B	ASN200
B	HIS297
B	TYR299

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1bqc

Chain	Residue	Details
C	GLU342
C	GLU201
C	ASN200
C	HIS297
C	TYR299

---