3RRX

Crystal Structure of Q683A mutant of Exo-1,3/1,4-beta-glucanase (ExoP) from Pseudoalteromonas sp. BB1

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	0008152	biological_process	metabolic process
A	0008422	molecular_function	beta-glucosidase activity
A	0009251	biological_process	glucan catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 901

Chain	Residue
A	GLU179
A	LEU592
A	ASN593
A	HOH822
A	HOH857
A	HOH878

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 902

Chain	Residue
A	ILE100
A	HOH853
A	HOH943
A	ALA92
A	ASP94
A	ASP98

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site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 1334

Chain	Residue
A	HOH1340

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Functional Information from PROSITE/UniProt

site_id	PS00775
Number of Residues	18
Details	GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLKnQlgfdGFVVSDwnA

Chain	Residue	Details
A	VAL279-ALA296

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