Structure of PDB 2pwe Chain B

Receptor sequence

>2pweB (length=556) Species: 265293 (Burkholderia ubonensis subsp. mesacidophila)

PGAPWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIWI
NPHYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDVV
INHSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAWE
KDPVTGQYYLHYFGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFDT
VATYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAVT
AGQIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLAD
FRQTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKALA
TVTLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKAT
AEELLTNVALTSRDNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAAR
EIGDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDGE
TYLVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQS
GIYKVK

3D structure

• PDB: 2pwe Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D99 R198 D200 Q254 H326 D327
• Catalytic site (residue number reindexed from 1): D98 R197 D199 Q253 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	GLC	B	D61 Y64 H104 F164 D200 Q254 H326 D327 R414	D60 Y63 H103 F163 D199 Q253 H325 D326 R413
BS02	FRU	B	F164 Q254 F256 D327 R414	F163 Q253 F255 D326 R413
BS03	CA	B	D22 N24 D26 I28 D30	D21 N23 D25 I27 D29

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

External links

• PDB: RCSB:2pwe, PDBe:2pwe, PDBj:2pwe
• PDBsum: 2pwe
• PubMed: 17597061
• UniProt: Q2PS28