Structure of PDB 4pzv Chain A

Receptor sequence
>4pzvA (length=413) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence]
MQYIIGIGTNIGFTIENIHLAITALESQQNIRIIRKASLYSSKAVLKEDA
PKEWDIRFLNTAVKISSSLKPDELLVLLKDIELKIGRDLNAPAWSPRVID
LDILAAEDLILETDKLTIPHKELINRSFALAPLLELSKGWHHPKYVEWDL
NIRLKELGEIVKLKQTLANTIRMGIVNLSSDGNFDDNQRKLNLDELIQSG
AEIIDIGAESTKPISIEEEFNKLDEFLEYFKSQLANLIYKPLVSIDTRKL
EVMQKILAKHHDIIWMINDVECNNIEQKAQLIAKYNKKYVIIHNLGITDR
NQYLDKENAIDNVCDYIEQKKQILLKHGIAQQNIYFDIGFGFGKKSDTAR
YLLENIIEIKRRLELKALVGHSRKPSVLGLAKDSNLATLDRATRELSRKL
EKLDIDIIRVHKI
3D structure
PDB4pzv Structural enzymology and inhibition of the bi-functional folate pathway enzyme HPPK-DHPS from the biowarfare agent Francisella tularensis.
ChainA
Resolution1.704 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R87 R97 D100 D102 K382 R417
Catalytic site (residue number reindexed from 1) R87 R97 D100 D102 K374 R409
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
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 J1D A V45 F58 N60 L75 K79 R87 W94 R97 D100 D102 I103 K115 L116 T117 H120 F128 V45 F58 N60 L75 K79 R87 W94 R97 D100 D102 I103 K115 L116 T117 H120 F128 MOAD: Kd=2uM
PDBbind-CN: -logKd/Ki=5.70,Kd=2.0uM
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0004156 dihydropteroate synthase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0016310 phosphorylation
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4pzv, PDBe:4pzv, PDBj:4pzv
PDBsum4pzv
PubMed24975935
UniProtQ5NGA7

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