2XFR

Crystal structure of barley beta-amylase at atomic resolution

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 PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1490

Chain	Residue
A	THR127
A	ASN129
A	PRO188
A	PRO191
A	TYR236
A	HOH2492
A	HOH2943

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1491

Chain	Residue
A	GLU228
A	PHE229
A	HOH2945
A	HOH2947
A	HOH2948
A	GLN212
A	PHE215

---

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

---