6KWC

Crystal Structure Analysis of Endo-beta-1,4-xylanase II

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	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 PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue GOL A 201

Chain	Residue
A	PHE62
A	SER63
A	THR133
A	THR188
A	VAL189
A	SER190
A	HOH307
A	HOH344

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site_id	AC2
Number of Residues	3
Details	binding site for residue IOD A 202

Chain	Residue
A	SER146
A	HOH509
A	ASN82

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site_id	AC3
Number of Residues	1
Details	binding site for residue IOD A 205

Chain	Residue
A	MET169

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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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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	GLN177

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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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