Structure of PDB 2ze0 Chain A

Receptor sequence
>2ze0A (length=531) Species: 258999 (Geobacillus sp. HTA-462) [Search protein sequence]
KKTWWKEGVAYQIYPRSFMDANGDGIGDLRGIIEKLDYLVELGVDIVWIC
PIYRSPNADNGYDISDYYAIMDEFGTMDDFDELLAQAHRRGLKVILDLVI
NHTSDEHPWFIESRSSRDNPKRDWYIWRDGKDGREPNNWESIFGGSAWQY
DERTGQYYLHIFDVKQPDLNWENSEVRQALYEMVNWWLDKGIDGFRIDAI
SHIKKKPGLPDLPLKYVPSFAGHMNQPGIMEYLRELKEQTFARYDIMTVG
EANGVTVDEAEQWVGEENGVFNMIFQFEHLGLWERRASIDVRRLKRTLTK
WQKGLENRGWNALFLENHDLPRSVSTWGNDRDYWAESAKALGALYFFMQG
TPFIYQGQEIGMTNVRFDDIRDYRDVSALRIIWKTGRDNSRTPMQWSGAS
NAGFTTGTPWIKVNENYRTINVEAERRDPNSVWSFYRQMIQLRKANELFV
YGTYDLLLENHPSIYAYTRTLGRDRALVVVNLSDRPSLYRYDGFRLQSSD
LALSNYPVRPHKNATRFKLKPYEARVYIWKE
3D structure
PDB2ze0 Crystal structure of GH13 alpha-glucosidase GSJ from one of the deepest sea bacteria
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D98 R197 D199 E256 H325 D326
Catalytic site (residue number reindexed from 1) D97 R196 D198 E251 H318 D319
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 D21 N23 D25 I27 D29 D20 N22 D24 I26 D28
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0043169 cation binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2ze0, PDBe:2ze0, PDBj:2ze0
PDBsum2ze0
PubMed18398906
UniProtQ33E90

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