Structure of PDB 2ypo Chain A

Receptor sequence

>2ypoA (length=458) Species: 1773 (Mycobacterium tuberculosis)

MNWTVDIPIDLPPLPTDLRTRLDAALAKPAAQQPTWPADQALAMRTVLES
VPPVTVPSEIVRLQEQLAQVAKGEAFLLQGGDCAETFMDNTEPHIRGNVR
ALLQMAVVLTYGASMPVVKVARIAGQYAKPRSADIDALGLRSYRGDMING
FAPDAAAREHDPSRLVRAYANASAAMNLVRALTSSGLASLHLVHDWNREF
VRTSPAGARYEALATEIDRGLRFMSACGVADRNLQTAEIYASHEALVLDY
ERAMLRLSDGDDGEPQLFDLSAHTVWIGERTRQIDGAHIAFAQVIANPVG
VKLGPNMTPELAVEYVERLDPHNKPGRLTLVSRMGNHKVRDLLPPIVEKV
QATGHQVIWQCDPMHGNTHESSTGFKTRHFDRIVDEVQGFFEVHRALGTH
PGGIHVEITGENVTECLGGAQDISETDLAGRYETACDPRLNTQQSLELAF
LVAEMLRD

3D structure

• PDB: 2ypo Three Sites and You are Out: Ternary Synergistic Allostery Controls Aromatic Aminoacid Biosynthesis in Mycobacterium Tuberculosis.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Enzyme Commision number: 2.5.1.54: 3-deoxy-7-phosphoheptulonate 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	MN	A	C87 H369 E411 D441	C83 H365 E407 D437
BS02	PHE	A	F91 M92 R171 A174 N175	F87 M88 R167 A170 N171	MOAD: Kd=21uM PDBbind-CN: -logKd/Ki=4.68,Kd=21uM

Gene Ontology

Molecular Function

• GO:0003849 3-deoxy-7-phosphoheptulonate synthase activity
• GO:0005515 protein binding
• GO:0016740 transferase activity
• GO:0030145 manganese ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0008652 amino acid biosynthetic process
• GO:0009073 aromatic amino acid family biosynthetic process
• GO:0009423 chorismate biosynthetic process
• GO:0051260 protein homooligomerization

Cellular Component

• GO:0005829 cytosol
• GO:0005886 plasma membrane
• GO:0009274 peptidoglycan-based cell wall

External links

• PDB: RCSB:2ypo, PDBe:2ypo, PDBj:2ypo
• PDBsum: 2ypo
• PubMed: 23274137
• UniProt: O53512|AROG_MYCTU Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (Gene Name=aroG)