Structure of PDB 3fyy Chain B

Receptor sequence
>3fyyB (length=375) Species: 221109 (Oceanobacillus iheyensis HTE831) [Search protein sequence]
MKITDLELHAVGIPRHTGFVNKHVIVKIHTDEGLTGIGEMSDFSHLPLYS
VDLHDLKQGLLSILLGQNPFDLMKINKELTDNFPETMYYYEKGSFIRNGI
DNALHDLCAKYLDISVSDFLGGRVKEKIKVCYPIFRHRFSEEVESNLDVV
RQKLEQGFDVFRLYVGKNLDADEEFLSRVKEEFGSRVRIKSYDFSHLLNW
KDAHRAIKRLTKYDLGLEMIESPAPRNDFDGLYQLRLKTDYPISEHVWSF
KQQQEMIKKDAIDIFNISPVFIGGLTSAKKAAYAAEVASKDVVLGTTQEL
SVGTAAMAHLGCSLTNINHTSDPTGPELYVGDVVKNRVTYKDGYLYAPDR
SVKGLGIELDESLLAKYQVPDLSWD
3D structure
PDB3fyy Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis .
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) D42 H45 Y90 P133 R162 Y164 Y192 D193 F194 M219 E221 S244 E245 H246 S268 G295 T296 T297 S321 D322
Catalytic site (residue number reindexed from 1) D42 H45 Y90 P133 R162 Y164 Y192 D193 F194 M219 E221 S244 E245 H246 S268 G295 T296 T297 S321 D322
Enzyme Commision number 4.2.1.158: galactarate dehydratase (D-threo-forming).
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 MG B D193 E221 H246 D193 E221 H246
BS02 MG B D42 H45 T297 D42 H45 T297
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3fyy, PDBe:3fyy, PDBj:3fyy
PDBsum3fyy
PubMed19883118
UniProtQ8EMJ9|GALRD_OCEIH Galactarate dehydratase (D-threo-forming) (Gene Name=OB2843)

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