Structure of PDB 1ud3 Chain A

Receptor sequence
>1ud3A (length=480) Species: 129736 (Bacillus sp. KSM-K38) [Search protein sequence]
DGLNGTMMQYYEWHLENDGQHWNRLHDDAAALSDAGITAIWIPPAYKGNS
QADVGYGAYDLYDLGEFNQKGTVRTKYGTKAQLERAIGSLKSNDINVYGD
VVMNHKMGADFTEAVQAVQVNPTNRWQDISGAYTIDAWTGFDFSGRNNAY
SDFKWRWFHFNGVDWDQRYQENHIFRFANTNWNWRVDEENGNYDYLLGSN
IDFSHPEVQDELKDWGSWFTDELDLDGYRLDAIKHIPFWYTSDWVRHQRN
EADQDLFVVGEYWKDDVGALEFYLDEMNWEMSLFDVPLHYNFYRASQQGG
SYDMRNILRGSLVEAHPMHAVTFVDNHDTQPGESLESWVADWFKPLAYAT
ILTREGGYPNVFYGDYYGIPNDNISAKKDMIDELLDARQNYAYGTQHDYF
DHWDVVGWTREGSSSRPNSGLATIMSNGPGGSKWMYVGRQNAGQTWTDLT
GNNGASVTINGDGWGEFFTNGGSVSVYVNQ
3D structure
PDB1ud3 Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D231 E261 D328
Catalytic site (residue number reindexed from 1) D231 E261 D328
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 NA A N104 D194 N200 H235 N104 D194 N200 H235
BS02 NA A G300 Y302 W403 D404 N427 G300 Y302 W403 D404 N427
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1ud3, PDBe:1ud3, PDBj:1ud3
PDBsum1ud3
PubMed12719434
UniProtQ93I48

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