3U7B

A new crystal structure of a Fusarium oxysporum GH10 xylanase reveals the presence of an extended loop on top of the catalytic cleft

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0031176	molecular_function	endo-1,4-beta-xylanase activity
A	0045493	biological_process	xylan catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005576	cellular_component	extracellular region
B	0005975	biological_process	carbohydrate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0031176	molecular_function	endo-1,4-beta-xylanase activity
B	0045493	biological_process	xylan catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005576	cellular_component	extracellular region
C	0005975	biological_process	carbohydrate metabolic process
C	0016787	molecular_function	hydrolase activity
C	0031176	molecular_function	endo-1,4-beta-xylanase activity
C	0045493	biological_process	xylan catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005576	cellular_component	extracellular region
D	0005975	biological_process	carbohydrate metabolic process
D	0016787	molecular_function	hydrolase activity
D	0031176	molecular_function	endo-1,4-beta-xylanase activity
D	0045493	biological_process	xylan catabolic process
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005576	cellular_component	extracellular region
E	0005975	biological_process	carbohydrate metabolic process
E	0016787	molecular_function	hydrolase activity
E	0031176	molecular_function	endo-1,4-beta-xylanase activity
E	0045493	biological_process	xylan catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:22751658

Chain	Residue	Details
A	GLU131
B	GLU131
C	GLU131
D	GLU131
E	GLU131

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site_id	SWS_FT_FI2
Number of Residues	5
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061, ECO:0000269|PubMed:22751658

Chain	Residue	Details
A	GLU245
B	GLU245
C	GLU245
D	GLU245
E	GLU245

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site_id	SWS_FT_FI3
Number of Residues	5
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22751658

Chain	Residue	Details
A	ASN101
B	ASN101
C	ASN101
D	ASN101
E	ASN101

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