2XG9

Crystal structure of Barley Beta-Amylase complexed with 4-O-alpha-D- glucopyranosylmoranoline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0016161	molecular_function	beta-amylase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

site_id	PS00506
Number of Residues	9
Details	BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD

Chain	Residue	Details
A	HIS91-ASP99

---

site_id	PS00679
Number of Residues	11
Details	BETA_AMYLASE_2 Beta-amylase active site 2. GpAGEMRYPSY

Chain	Residue	Details
A	GLY180-TYR190

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P10538","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P10538","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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