Structure of PDB 2xg9 Chain A

Receptor sequence

>2xg9A (length=487) Species: 4513 (Hordeum vulgare)

VNVKGNYVQVYVMLPLDAVSVNNRFEKGDELRAQLRKLVEAGVDGVMVDV
WWGLVEGKGPKAYDWSAYKQLFELVQKAGLKLQAIMSFHQCGGNVGDAVN
IPIPQWVRDVGTRDPDIFYTDGHGTRNIEYLTLGVDNQPLFHGRSAVQMY
ADYMTSFRENMKEFLDAGVIVDIEVGLGPAGEMRYPSYPQSHGWSFPGIG
EFICYDKYLQADFKAAAAAVGHPEWEFPNDVGQYNDTPERTQFFRDNGTY
LSEKGRFFLAWYSNNLIKHGDRILDEANKVFLGYKVQLAIKISGIHWWYK
VPSHAAELTAGYYNLHDRDGYRTIARMLKRHRASINFTCAEMRDSEQSSQ
AMSAPEELVQQVLSAGWREGLNVACENALPRYDPTAYNTILRNARPHGIN
QSGPPEHKLFGFTYLRLSNQLVEGQNYANFKTFVDRMHANLPRDPYVDPM
APLPRSGPEISIEMILQAAQPKLQPFPFQEHTDLPVG

3D structure

• PDB: 2xg9 Chemical Genetics and Cereal Starch Metabolism: Structural Basis of the Non-Covalent and Covalent Inhibition of Barley Beta-Amylase.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D99 E184 T340 E378 L381
• Catalytic site (residue number reindexed from 1): D97 E182 T338 E376 L379
• 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	NOJ	A	E184 E378 A380	E182 E376 A378	PDBbind-CN: -logKd/Ki=4.15,Ki=70uM
BS02	GLC	A	M15 D51 H91 R418	M13 D49 H89 R416	PDBbind-CN: -logKd/Ki=4.15,Ki=70uM

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

External links

• PDB: RCSB:2xg9, PDBe:2xg9, PDBj:2xg9
• PDBsum: 2xg9
• PubMed: 21085740
• UniProt: P16098|AMYB_HORVU Beta-amylase (Gene Name=BMY1)