Structure of PDB 2pwd Chain B

Receptor sequence
>2pwdB (length=557) Species: 265293 (Burkholderia ubonensis subsp. mesacidophila) [Search protein sequence]
KPGAPWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIW
INPHYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDV
VINHSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAW
EKDPVTGQYYLHYFGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFD
TVATYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAV
TAGEIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLA
DFRQTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKAL
ATVTLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKA
TAEELLTNVALTSRDNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAA
REIGDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDG
ETYLVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQ
SGIYKVK
3D structure
PDB2pwd Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.
ChainB
Resolution1.8 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) D99 R198 D200 E254 H326 D327
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 B D22 N24 D26 I28 D30 D22 N24 D26 I28 D30
BS02 NOJ B D61 Y64 H104 F164 D200 E254 H326 D327 R414 D61 Y64 H104 F164 D200 E254 H326 D327 R414 MOAD: Ki=40uM
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:2pwd, PDBe:2pwd, PDBj:2pwd
PDBsum2pwd
PubMed17597061
UniProtQ2PS28

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