Structure of PDB 2wcv Chain F

Receptor sequence
>2wcvF (length=140) Species: 562 (Escherichia coli) [Search protein sequence]
MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLV
SDLLQAIIPLFELDSYAPPLVMMAAVEGDTLDPEVERRYRNALSLQAPCP
DIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP
3D structure
PDB2wcv Crystal Structures and Enzyme Mechanism of a Dual Fucose Mutarotase/Ribose Pyranase
ChainF
Resolution1.9 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 5.1.3.29: L-fucose mutarotase.
5.4.99.62: D-ribose pyranase.
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 FUC F D30 H32 F33 M73 Y111 K128 Y129 D30 H32 F33 M73 Y111 K128 Y129 MOAD: Kd=1.7mM
BS02 FUC F H22 Y66 H22 Y66 MOAD: Kd=1.7mM
Gene Ontology
Molecular Function
GO:0016853 isomerase activity
GO:0016854 racemase and epimerase activity
GO:0016857 racemase and epimerase activity, acting on carbohydrates and derivatives
GO:0036373 L-fucose mutarotase activity
GO:0042802 identical protein binding
GO:0042806 fucose binding
GO:0048029 monosaccharide binding
GO:0062193 D-ribose pyranase activity
Biological Process
GO:0005996 monosaccharide metabolic process
GO:0006004 fucose metabolic process
GO:0036065 fucosylation
GO:0042354 L-fucose metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2wcv, PDBe:2wcv, PDBj:2wcv
PDBsum2wcv
PubMed19524593
UniProtP0AEN8|FUCM_ECOLI L-fucose mutarotase (Gene Name=fucU)

[Back to BioLiP]