Structure of PDB 1eye Chain A

Receptor sequence

>1eyeA (length=256) Species: 83332 (Mycobacterium tuberculosis H37Rv)

PVQVMGVLNVTDDSFSDGGCYLDLDDAVKHGLAMAAAGAGIVDVGGETSR
VIPVVKELAAQGITVSIDTMRADVARAALQNGAQMVNDVSGGRADPAMGP
LLAEADVPWVLMHWRAVSADTPHVPVRYGNVVAEVRADLLASVADAVAAG
VDPARLVLDPGLGFAKTAQHNWAILHALPELVATGIPVLVGASRKRFLGA
LLAGPDGVMRPTDGRDTATAVISALAALHGAWGVRVHDVRASVDAIKVVE
AWMGAE

3D structure

• PDB: 1eye Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K213 R253
• Catalytic site (residue number reindexed from 1): K195 R235
• Enzyme Commision number: 2.5.1.15: dihydropteroate 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	MG	A	N13 D21 H255	N9 D17 H237
BS02	PMM	A	D21 D86 N105 V107 M130 D177 F182 G209 K213 R253 H255	D17 D68 N87 V89 M112 D159 F164 G191 K195 R235 H237

Gene Ontology

Molecular Function

• GO:0004156 dihydropteroate synthase activity
• GO:0016740 transferase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009396 folic acid-containing compound biosynthetic process
• GO:0042558 pteridine-containing compound metabolic process
• GO:0044237 cellular metabolic process
• GO:0046654 tetrahydrofolate biosynthetic process
• GO:0046656 folic acid biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1eye, PDBe:1eye, PDBj:1eye
• PDBsum: 1eye
• PubMed: 11007651
• UniProt: P9WND1|DHPS1_MYCTU Dihydropteroate synthase (Gene Name=folP1)