Structure of PDB 3mio Chain A

Receptor sequence
>3mioA (length=195) Species: 419947 (Mycobacterium tuberculosis H37Ra) [Search protein sequence]
MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMV
RYTSGYLCVPLDGAICDRLGLLPMYTVTVDARNGIGTGISASDRATTMRL
LADPTSVADDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARMAGLQPAG
AICEIVSQKDEGSMAHTDELRVFADEHGLALITIADLIEWRRKHE
3D structure
PDB3mio Structural basis for pH dependent monomer-dimer transition of 3,4-dihydroxy 2-butanone-4-phosphate synthase domain from Mycobacterium tuberculosis
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E29 D33 C58 Y86 D91 H127 H144 E165
Catalytic site (residue number reindexed from 1) E29 D33 C58 Y75 D80 H116 H133 E154
Enzyme Commision number 3.5.4.25: GTP cyclohydrolase II.
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 PO4 A D5 S6 R9 D5 S6 R9
BS02 PO4 A R141 G143 H144 T145 R130 G132 H133 T134
Gene Ontology
Molecular Function
GO:0008686 3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Biological Process
GO:0009231 riboflavin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3mio, PDBe:3mio, PDBj:3mio
PDBsum3mio
PubMed21296160
UniProtA5U2B7|RIBBA_MYCTA Riboflavin biosynthesis protein RibBA (Gene Name=ribBA)

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