1K72

The X-ray Crystal Structure Of Cel9G Complexed With cellotriose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0030246	molecular_function	carbohydrate binding
A	0030248	molecular_function	cellulose binding
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0030246	molecular_function	carbohydrate binding
B	0030248	molecular_function	cellulose binding

Functional Information from PROSITE/UniProt

site_id	PS00592
Number of Residues	25
Details	GH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. YALGsTgr..SFVVGy....GvnPPqhPHHR

Chain	Residue	Details
A	TYR351-ARG375

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site_id	PS00698
Number of Residues	19
Details	GH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. YtDeinnYvnnEiAcdyNA

Chain	Residue	Details
A	TYR409-ALA427

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site_id	PS60032
Number of Residues	18
Details	GH9_1 Glycosyl hydrolases family 9 (GH9) active site signature 1. LtGGWYDAGDhvKFnLPM

Chain	Residue	Details
A	LEU49-MET66

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10140

Chain	Residue	Details
A	ASP58
B	ASP58

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10059

Chain	Residue	Details
A	HIS373
B	HIS373

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site_id	SWS_FT_FI3
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060

Chain	Residue	Details
A	ASP411
A	GLU420
B	ASP411
B	GLU420

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