Structure of PDB 1e7q Chain A

Receptor sequence
>1e7qA (length=314) Species: 562 (Escherichia coli) [Search protein sequence]
KQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFA
SERIDQVYLAAAKVGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKL
LFLGASCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNR
QYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRFHEATAQSAPDVVVW
GSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPMLSHINVGTGVDCT
IRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLE
AGLASTYQWFLENQ
3D structure
PDB1e7q Probing the Catalytic Mechanism of Gdp-4-Keto-6-Deoxy-D-Mannose Epimerase/Reductase by Kinetic and Crystallographic Characterization of Site-Specific Mutants
ChainA
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) A107 S108 C109 Y136 K140 H179
Catalytic site (residue number reindexed from 1) A105 S106 C107 Y134 K138 H177
Enzyme Commision number 1.1.1.271: GDP-L-fucose 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 NAP A G13 M14 V15 R36 L41 A63 A64 V66 L105 G106 A107 Y136 K140 P163 T164 N165 L166 G11 M12 V13 R34 L39 A61 A62 V64 L103 G104 A105 Y134 K138 P161 T162 N163 L164
BS02 UVW A G68 I69 V70 A71 S178 G66 I67 V68 A69 S176
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016853 isomerase activity
GO:0042803 protein homodimerization activity
GO:0050577 GDP-L-fucose synthase activity
GO:0070401 NADP+ binding
Biological Process
GO:0009226 nucleotide-sugar biosynthetic process
GO:0009242 colanic acid biosynthetic process
GO:0042351 'de novo' GDP-L-fucose biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1e7q, PDBe:1e7q, PDBj:1e7q
PDBsum1e7q
PubMed11021971
UniProtP32055|FCL_ECOLI GDP-L-fucose synthase (Gene Name=fcl)

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