Structure of PDB 1hvx Chain A

Receptor sequence

>1hvxA (length=483) Species: 1422 (Geobacillus stearothermophilus)

AAPFNGTMMQYFEWYLPDDGTLWTKVANEANNLSSLGITALWLPPAYKGT
SRSDVGYGVYDLYDLGEFNQKGAVRTKYGTKAQYLQAIQAAHAAGMQVYA
DVVFDHKGGADGTEWVDAVEVNPSDRNQEISGTYQIQAWTKFDFPGRGNT
YSSFKWRWYHFDGVDWDESRKLSRIYKFRGIGKAWDWEVDTENGNYDYLM
YADLDMDHPEVVTELKSWGKWYVNTTNIDGFRLDAVKHIKFSFFPDWLSY
VRSQTGKPLFTVGEYWSYDINKLHNYIMKTNGTMSLFDAPLHNKFYTASK
SGGTFDMRTLMTNTLMKDQPTLAVTFVDNHDTEPGQALQSWVDPWFKPLA
YAFILTRQEGYPCVFYGDYYGIPQYNIPSLKSKIDPLLIARRDYAYGTQH
DYLDHSDIIGWTREGVTEKPGSGLAALITDGPGGSKWMYVGKQHAGKVFY
DLTGNRSDTVTINSDGWGEFKVNGGSVSVWVPR

3D structure

• PDB: 1hvx Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D234 E264 D331
• Catalytic site (residue number reindexed from 1): D234 E264 D331
• Enzyme Commision number: 3.2.1.1: alpha-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	CA	A	D162 A184 D186 D205	D162 A184 D186 D205
BS02	CA	A	D105 D197 D203 H238	D105 D197 D203 H238
BS03	CA	A	G303 F305 S406 D407 D430	G303 F305 S406 D407 D430

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0004556 alpha-amylase activity
• GO:0005509 calcium ion binding
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:1hvx, PDBe:1hvx, PDBj:1hvx
• PDBsum: 1hvx
• PubMed: 11226887
• UniProt: P06279|AMY_GEOSE Alpha-amylase (Gene Name=amyS)