Structure of PDB 4p8e Chain B

Receptor sequence
>4p8eB (length=217) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
SHMNQSSLLAEFGDPITRVENALQALREGRGVLLLDDEDRENEGDIIYAV
ESLTTAQMALMIRECSGIVCLCLTEAQADRLALPPMVVNNNSANQTAFTV
SIEAKHGVTTGVSAQDRVTTIKTAANPQAKPEDLARPGHVFPLRARAGGV
LARRGHTEGTVDLMQMAGLQPAGVLCELTNPDGSMAKTPEIIEFGKLHNM
PVLTIEDMVQYRIQFDL
3D structure
PDB4p8e Structural Basis for Competitive Inhibition of 3,4-Dihydroxy-2-butanone-4-phosphate Synthase from Vibrio cholerae.
ChainB
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E39 D43 C68 N92 F96 E101 H137 H154 E175
Catalytic site (residue number reindexed from 1) E41 D45 C70 N94 F98 E103 H139 H156 E177
Enzyme Commision number 4.1.99.12: 3,4-dihydroxy-2-butanone-4-phosphate 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 5RP B R38 E39 D43 C68 T94 F96 R151 G153 H154 T155 L173 E175 R40 E41 D45 C70 T96 F98 R153 G155 H156 T157 L175 E177
BS02 ZN B E39 H154 E41 H156
BS03 ZN B E62 H196 E64 H198
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0008686 3,4-dihydroxy-2-butanone-4-phosphate synthase activity
GO:0016829 lyase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009231 riboflavin biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4p8e, PDBe:4p8e, PDBj:4p8e
PDBsum4p8e
PubMed25792735
UniProtQ9KKP2|RIBB_VIBCH 3,4-dihydroxy-2-butanone 4-phosphate synthase (Gene Name=ribB)

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