Structure of PDB 2die Chain A

Receptor sequence

>2dieA (length=481) Species: 1409 (Bacillus sp. (in: firmicutes))

TNGTMMQYFEWHLPNDGNHWNRLRDDAANLKSKGITAVWIPPAWKGTSQN
DVGYGAYDLYDLGEFNQKGTVRTKYGTRSQLQGAVTSLKNNGIQVYGDVV
MNHKGGADGTEMVNAVEVNRSNRNQEISGEYTIEAWTKFDFPGRGNTHSN
FKWRWYHFDGTDWDQSRQLQNKIYKFRGTGKAWDWEVDIENGNYDYLMYA
DIDMDHPEVINELRNWGVWYTNTLNLDGFRIDAVKHIKYSYTRDWLTHVR
NTTGKPMFAVAEFWKNDLAAIENYLNKTSWNHSVFDVPLHYNLYNASNSG
GYFDMRNILNGSVVQKHPIHAVTFVDNHDSQPGEALESFVQSWFKPLAYA
LILTREQGYPSVFYGDYYGIPTHGVPSMKSKIDPLLQARQTYAYGTQHDY
FDHHDIIGWTREGDSSHPNSGLATIMSDGPGGNKWMYVGKHKAGQVWRDI
TGNRSGTVTINADGWGNFTVNGGAVSVWVKQ

3D structure

• PDB: 2die Ancestral sequence evolutionary trace and crystal structure analyses of alkaline alpha-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D236 E266 D333
• Catalytic site (residue number reindexed from 1): D232 E262 D329
• 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	D163 A186 D188 D207	D159 A182 D184 D203
BS02	CA	A	N106 D199 D205 H240	N102 D195 D201 H236
BS03	CA	A	G305 F307 H408 D409 D432	G301 F303 H404 D405 D428
BS04	NA	A	D163 D188 D199 D205 I206 D207	D159 D184 D195 D201 I202 D203

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0005509 calcium ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:2die, PDBe:2die, PDBj:2die
• PDBsum: 2die
• PubMed: 17154418
• UniProt: O82839