5ZO0

Neutron structure of xylanase at pD5.4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0005576	cellular_component	extracellular region
A	0008152	biological_process	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. PLiEYYIVEnF

Chain	Residue	Details
A	PRO83-PHE93

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

Chain	Residue	Details
A	VAL174-ALA185

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374

Chain	Residue	Details
A	GLU86

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374

Chain	Residue	Details
A	GLU177

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:24419374

Chain	Residue	Details
A	TYR73
A	TYR77
A	TYR88
A	ARG122
A	PRO126
A	GLN136
A	TYR171

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN38
A	ASN61

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