2B45

Crystal structure of an engineered uninhibited Bacillus subtilis xylanase in free state

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0000272	biological_process	polysaccharide catabolic process
X	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
X	0005975	biological_process	carbohydrate metabolic process
X	0016787	molecular_function	hydrolase activity
X	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
X	0031176	molecular_function	endo-1,4-beta-xylanase activity
X	0045493	biological_process	xylan catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EPE X 1001

Chain	Residue
X	GLN7
X	TRP9
X	TYR69
X	GLU78
X	SER117
X	ILE118
X	TYR166
X	GLU172
X	HOH1097

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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. PLiEYYVVDsW

Chain	Residue	Details
X	PRO75-TRP85

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

Chain	Residue	Details
X	MET169-SER180

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:7911679

Chain	Residue	Details
X	GLU78

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063

Chain	Residue	Details
X	GLU172

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Catalytic Information from CSA

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

Chain	Residue	Details
X	GLU172
X	GLU78

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