1H41

Pseudomonas cellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0008152	biological_process	metabolic process
A	0009279	cellular_component	cell outer membrane
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0033939	molecular_function	xylan alpha-1,2-glucuronosidase activity
A	0045493	biological_process	xylan catabolic process
A	0046559	molecular_function	alpha-glucuronidase activity
A	2000886	biological_process	glucuronoxylan catabolic process
B	0000272	biological_process	polysaccharide 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	0008152	biological_process	metabolic process
B	0009279	cellular_component	cell outer membrane
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0033939	molecular_function	xylan alpha-1,2-glucuronosidase activity
B	0045493	biological_process	xylan catabolic process
B	0046559	molecular_function	alpha-glucuronidase activity
B	2000886	biological_process	glucuronoxylan catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:11937059

Chain	Residue	Details
A	ALA292
B	ALA292

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11937059

Chain	Residue	Details
A	ASP365
A	GLU393
B	ASP365
B	GLU393

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site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
A	LYS288
A	ARG325
A	ARG336
A	LYS360
A	HIS521
A	TRP543
B	GLU168
B	ASN211
B	LYS288
B	ARG325
B	ARG336
B	LYS360
B	HIS521
B	TRP543
A	ASN211
A	GLU168

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLU387
B	GLU387

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site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA

Chain	Residue	Details
B	TRP160
B	TRP543
A	TRP543
A	TRP160

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