Structure of PDB 5a2b Chain A

Receptor sequence
>5a2bA (length=452) [Search protein sequence]
ERTWQDERIYFIMVDRFNNGNPKNDYEVDVHDPKAYHGGDLQGIIDKLDY
IKEMGFTAIWLTPIFANEKGGYHGYWIEDFYKVEEHFGTLDDFKRLVKEA
HKRDMKVILDFVVNHTGYNHPWLNDPAKKDWFHEKKDIFNWANQQEVENG
WLFGLPDLAQENPEVKTYLFDVAKWWIQETDIDGYRLDTVKHVPKWFWDE
FAKEVKSVKQDFFLLGEVWHDDPRYVAEYGKHGIDALIDFPFYKEASTIF
SNVDQSLEPLYNVWKRNVAFYERPYLLGTFLDNHDTVRFTRLALQNRINP
VTRLKLGLTYLFSAPGIPIMYYGTEIALDGGEDPDNRRLMNFRTDKELID
YVTKLGELRAKLPSLRRGDFELLYEKDGMALFKRTYEKETTVIAINNTSK
TQKVTLDGELEQGKELRGLLAGDLVRSKDGKYDIILDRETAEIYVLAPKT
GL
3D structure
PDB5a2b Crystal Structure of Anoxybacillus Alpha-Amylase Provides Insights Into Maltose Binding of a New Glycosyl Hydrolase Subclass.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D135 R211 D213 E242 H309 D310
Catalytic site (residue number reindexed from 1) D110 R186 D188 E217 H284 D285
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 GLC A Y100 H140 D213 T214 E242 H309 D310 Y75 H115 D188 T189 E217 H284 D285
BS02 GLC A H98 Y100 W101 D358 R362 H73 Y75 W76 D333 R337
BS03 CA A N139 E173 D182 H217 N114 E148 D157 H192
BS04 CA A N44 N46 N49 D50 G63 D65 N19 N21 N24 D25 G38 D40
BS05 CA A N92 E109 N67 E84
Gene Ontology
Molecular Function
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:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5a2b, PDBe:5a2b, PDBj:5a2b
PDBsum5a2b
PubMed26975884
UniProtI1VWH9

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