Structure of PDB 1b1y Chain A

Receptor sequence
>1b1yA (length=500) Species: 4513 (Hordeum vulgare) [Search protein sequence]
MKGNYVQVYVMLPLDAVSVNNRFEKGDELRAQLRKLVEAGVDGVMVDVWW
GLVEGKGPKAYDWSAYKQLFELVQKAGLKLQAIMSFHQCGGNVGDAVNIP
IPQWVRDVGTRDPDIFYTDGHGTRNIEYLTLGVDNQPLFHGRSAVQMYAD
YMTSFRENMKDFLDAGVIVDIEVGLGPAGELRYPSYPQSHGWSFPGIGEF
ICYDKYLQADFKAAAAAVGHPEWEFPNDAGQYNDTPERTQFFRDNGTYLS
EKGRFFLAWYSNNLIKHGDRILDEANKVFLGYKVQLAIKIAGVHWWYKVP
SHAAELTAGYYNLHDRDGYRTIARMLKRHRASINFTCAEMRDSEQPPDAM
SAPEELVQQVLSAGWREGLNVSCENALPRYDPTAYNTILRNARPHGINQS
GPPEHKLFGFTYLRLSNQLVEGQNYVNFKTFVDRMHANLPRDPYVDPMAP
LPRSGPEISIEMILQAAQPKIQPFPFQEHTDLPVGPTGGMGGQAEGPTCG
3D structure
PDB1b1y The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D99 E184 T340 E378 L381
Catalytic site (residue number reindexed from 1) D95 E180 T336 E374 L377
Enzyme Commision number 3.2.1.2: beta-amylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 BGC A A182 E184 K293 T340 E378 A380 A178 E180 K289 T336 E374 A376
BS02 GLC A M15 D51 H91 D99 A182 R418 M11 D47 H87 D95 A178 R414
Gene Ontology
Molecular Function
GO:0016161 beta-amylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0042802 identical protein binding
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1b1y, PDBe:1b1y, PDBj:1b1y
PDBsum1b1y
PubMed9918723
UniProtP16098|AMYB_HORVU Beta-amylase (Gene Name=BMY1)

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