Structure of PDB 2dzb Chain A

Receptor sequence
>2dzbA (length=251) Species: 274 (Thermus thermophilus) [Search protein sequence]
VRTLWLRDRALDLDRVRLLGVLNLTPRALERAREMVAEGADILDLGAESE
EEKRRLLPVLEAVLSLGVPVSVDTRKPEVAEEALKLGAHLLNDVTGLRDE
RMVALAARHGVAAVVMHMPVPDPATMMAHARYRDVVAEVKAFLEAQARRA
LSAGVPQVVLDPGFGFGKLLEHNLALLRRLDEIVALGHPVLVGLSRKRTI
GELSGVEDPAQRVHGSVAAHLFAVMKGVRLLRVHDVRAHREALGVWEALY
G
3D structure
PDB2dzb Crystal Structure of Dihydropteroate Synthase (FolP) from Thermus thermophilus HB8
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K233 R268
Catalytic site (residue number reindexed from 1) K197 R232
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 HH2 A N36 D109 N128 M152 D197 F202 K233 R268 H270 N23 D73 N92 M116 D161 F166 K197 R232 H234
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

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Cellular Component
External links
PDB RCSB:2dzb, PDBe:2dzb, PDBj:2dzb
PDBsum2dzb
PubMed
UniProtQ5SLV2

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