1PVX

DO-1,4-BETA-XYLANASE, ROOM TEMPERATURE, PH 4.5

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	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031176	molecular_function	endo-1,4-beta-xylanase activity
A	0045493	biological_process	xylan catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00776
Number of Residues	11
Details	GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEYYIVEnF

Chain	Residue	Details
A	PRO83-PHE93

---

site_id	PS00777
Number of Residues	12
Details	GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VatEGYFSSGyA

Chain	Residue	Details
A	VAL175-ALA186

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	190
Details	Domain: {"description":"GH11","evidences":[{"source":"PROSITE-ProRule","id":"PRU01097","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10062","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10063","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"10623548","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1bvv

Chain	Residue	Details
A	GLU86
A	GLU178

---