Structure of PDB 1w9x Chain A

Receptor sequence
>1w9xA (length=481) Species: 79882 (Sutcliffiella halmapala) [Search protein sequence]
TNGTMMQYFEWHLPNDGQHWNRLRDDASNLRNRGITAIWIPPAWKGTSQN
DVGYGAYDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVV
MNHKGGADATENVLAVEVNPNNRNQEISGDYTIEAWTKFDFPGRGNTYSD
FKWRWYHFDGVDWDQSRQFQNRIYKFRGDGKAWDWEVDSENGNYDYLMYA
DVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKHIKYSFTRDWLTHVR
NATGKEMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNASNSG
GNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYA
LILTREQGYPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDY
FDHHNIIGWTREGNTTHPNSGLATIMSDGPGGEKWMYVGQNKAGQVWHDI
TGNKPGTVTINADGWANFSVNGGSVSIWVKR
3D structure
PDB1w9x Structure of a Bacillus Halmapalus Family 13 Alpha-Amylase, Bha, in Complex with an Acarbose-Derived Nonasaccharide at 2.1 A Resolution
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0043169 cation binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1w9x, PDBe:1w9x, PDBj:1w9x
PDBsum1w9x
PubMed15681870
UniProtO82839

[Back to BioLiP]