Structure of PDB 2pwf Chain A

Receptor sequence
>2pwfA (length=555) Species: 265293 (Burkholderia ubonensis subsp. mesacidophila) [Search protein sequence]
GAPWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIWIN
PHYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDVVI
NHSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAWEK
DPVTGQYYLHYFGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFATV
ATYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAVTA
GEIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLADF
RQTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKALAT
VTLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKATA
EELLTNVALTSRDNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAARE
IGDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDGET
YLVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQSG
IYKVK
3D structure
PDB2pwf Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.
ChainA
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 A200 E254 H326 D327
Catalytic site (residue number reindexed from 1) D97 R196 A198 E252 H324 D325
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 BGC A D61 Y64 H104 F164 R198 A200 E254 H326 D327 R414 D59 Y62 H102 F162 R196 A198 E252 H324 D325 R412
BS02 CA A D22 N24 D26 I28 D30 D20 N22 D24 I26 D28
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
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Biological Process
External links
PDB RCSB:2pwf, PDBe:2pwf, PDBj:2pwf
PDBsum2pwf
PubMed17597061
UniProtQ2PS28

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