Structure of PDB 3fxg Chain D

Receptor sequence
>3fxgD (length=405) Species: 229533 (Fusarium graminearum PH-1) [Search protein sequence]
SVKDFPKIKAIRSFIIGGVGSGGDYHNVKGGHWLIDSDISTPASKWEQYK
KSRTSWGINVLGSFLVEIEATDGTVGFATGFGGPPACWLVHQHFERFLIG
ADPRNTNLLFEQMYRASMFYGRKGLPIAVISVIDLALWDLLGKVRNEPVY
RLIGGATKERLDFYCTGPEPTAAKAMGFWGGKVPLPFCPDDGHEGLRKNV
EFLRKHREAVGPDFPIMVDCYMSLNVSYTIELVKACLDLNINWWEECLSP
DDTDGFALIKRAHPTVKFTTGEHEYSRYGFRKLVEGRNLDIIQPDVMWLG
GLTELLKVAALAAAYDVPVVPHASGPYSYHFQISQPNTPFQEYLANSPDG
KSVLPVFGDLFIDEPIPTKGYLTTADLDKPGFGLTINPAARAKLIPSDYL
FKVPE
3D structure
PDB3fxg Crystal structure of rhamnonate dehydratase from Gibberella zeae complexed with Mg
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K184 P186 E196 D221 Y223 E247 G273 E274 Q295 D297 H324 E344
Catalytic site (residue number reindexed from 1) K182 P184 E194 D219 Y221 E245 G271 E272 Q293 D295 H322 E342
Enzyme Commision number ?
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 D D221 E247 E274 D219 E245 E272
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:0050032 L-rhamnonate dehydratase activity
Biological Process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3fxg, PDBe:3fxg, PDBj:3fxg
PDBsum3fxg
PubMed
UniProtD0VX14

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