Structure of PDB 2pwg Chain A

Receptor sequence
>2pwgA (length=556) Species: 265293 (Burkholderia ubonensis subsp. mesacidophila) [Search protein sequence]
PGAPWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIWI
NPHYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDVV
INHSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAWE
KDPVTGQYYLHYFGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFDT
VATYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAVT
AGEIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLAD
FRQTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKALA
TVTLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKAT
AEELLTNVALTSRDNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAAR
EIGDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDGE
TYLVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQS
GIYKVK
3D structure
PDB2pwg Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D99 R198 D200 E254 H326 D327
Catalytic site (residue number reindexed from 1) D98 R197 D199 E253 H325 D326
Enzyme Commision number 5.4.99.11: isomaltulose synthase.
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 D22 N24 D26 I28 D30 D21 N23 D25 I27 D29
BS02 CTS A D61 Y64 H104 F164 D200 E254 D327 R414 D60 Y63 H103 F163 D199 E253 D326 R413 MOAD: Ki=15uM
PDBbind-CN: -logKd/Ki=4.82,Ki=15uM
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2pwg, PDBe:2pwg, PDBj:2pwg
PDBsum2pwg
PubMed17597061
UniProtQ2PS28

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