Structure of PDB 3a9s Chain C

Receptor sequence
>3a9sC (length=589) Species: 33936 (Aeribacillus pallidus) [Search protein sequence]
AKDPRYVGNLPKIGIRPTIDGRRKGVRESLEETTMNMAKAVAKLLEENVF
YYNGQPVECVIADTCIGGVKEAAEAAEKFAREGVGVSITVTPCWCYGTET
MDMDPHIPKAVWGFNGTERPGAVYLAAVLAGYNQKGLPAFGIYGKDVQDA
GDTNIPEDVKEKLIRFAKAGLAVAMMKGKSYLSIGSVSMGIAGSVVQEDF
FQNYLGMRNEYVDMSEFVRRIELGIYDKEEYERALKWVKENCKVGPDNNR
DGFKRTEEQKEKDWEISVKMALIARDLMVGNKKLEEMGYGEEALGRNAIV
AGFQGQRQWTDYFPNGDFMETILNSSFDWNGKRAPYIFATENDNLNGISM
LFGYLLTNTAQIFADVRTYWSPEAVKRVTGYTLEGRAANGIIHLINSGAA
ALDGTGEQTKDGKPVIKPYYELTDEDIKKCLEATQFRPASTEYFRGGGYS
TDFLTKGGMPVTISRLNIVKGLGPVLQIAEGYTVDLPEEVHDVLDKRTDP
TWPTTWFVPNLTGEGAFKDVYSVMNNWGANHCSISYGHIGADLITLASIL
RIPVNMHNVPEEKIFRPDAWSMFGTKDLEGADYRACKKL
3D structure
PDB3a9s X-ray structures of Bacillus pallidusd-arabinose isomerase and its complex with l-fucitol.
ChainC
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E342 D366 H532
Catalytic site (residue number reindexed from 1) E341 D365 H531
Enzyme Commision number 5.3.1.25: L-fucose isomerase.
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 MN C E342 D366 H532 E341 D365 H531
BS02 GOL C M190 Q307 D366 M189 Q306 D365
BS03 GOL C V50 F51 K169 L357 T358 N359 V49 F50 K168 L356 T357 N358
Gene Ontology
Molecular Function
GO:0008736 L-fucose isomerase activity
GO:0008790 arabinose isomerase activity
GO:0016853 isomerase activity
GO:0016861 intramolecular oxidoreductase activity, interconverting aldoses and ketoses
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0005996 monosaccharide metabolic process
GO:0006004 fucose metabolic process
GO:0019317 fucose catabolic process
GO:0019571 D-arabinose catabolic process
GO:0042355 L-fucose catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3a9s, PDBe:3a9s, PDBj:3a9s
PDBsum3a9s
PubMed20123133
UniProtC0SSE7

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