Structure of PDB 4i14 Chain A

Receptor sequence

>4i14A (length=325) Species: 419947 (Mycobacterium tuberculosis H37Ra)

MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMV
RYTSGYLCVPLDGAICDRLGLLPMYAYTVTVDARNGIGTGISASDRATTM
RLLADPTSVADDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARMAGLQP
AGAICEIVSQKDEGSMAHTDELRVFADEHGLALITIADLIEWRRKHEKHI
ERVAEARIPTRHGEFRAIGYTSIYEDVEHVALVRGEIAGDGDDVLVRVHS
ECLTGDVFGSRRCDCGPQLDAALAMVAREGRGVVLYMRYGIGAQILVDLG
VRSMRLLTNNPDGYGLHIIERVPLP

3D structure

• PDB: 4i14 The crystal structure reveals the molecular mechanism of bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (Rv1415) from Mycobacterium tuberculosis
• Chain: A
• Resolution: 3.0 Å

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 Y77 D82 H118 H135 E156
• 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	ZN	A	C264 C275 C277	C252 C263 C265

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0003935 GTP cyclohydrolase II activity
• GO:0005525 GTP binding
• GO:0008270 zinc ion binding
• GO:0008686 3,4-dihydroxy-2-butanone-4-phosphate synthase activity
• GO:0016787 hydrolase 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

External links

• PDB: RCSB:4i14, PDBe:4i14, PDBj:4i14
• PDBsum: 4i14
• PubMed: 23999287
• UniProt: A5U2B7|RIBBA_MYCTA Riboflavin biosynthesis protein RibBA (Gene Name=ribBA)