Structure of PDB 1cbk Chain A

Receptor sequence
>1cbkA (length=160) Species: 727 (Haemophilus influenzae) [Search protein sequence]
MITAYIALGSNLNTPVEQLHAALKAISQLSNTHLVTTSSFYKSKPLGPQD
QPDYVNAVAKIETELSPLKLLDELQRIENEQGRVRLRRWGERTLDLDILL
YGNEIIQNERLTIPHYDMHNREFVIVPLFEIASDLVLPNSQIITELVKQF
ADHKMIKLNP
3D structure
PDB1cbk The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae.
ChainA
Resolution2.02 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R83 R92 D95 D97
Catalytic site (residue number reindexed from 1) R83 R92 D95 D97
Enzyme Commision number 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 SO4 A R85 R88 W89 R92 R85 R88 W89 R92
BS02 ROI A K44 L46 Y54 N56 W89 R92 F123 K44 L46 Y54 N56 W89 R92 F123
Gene Ontology
Molecular Function
GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0016310 phosphorylation
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1cbk, PDBe:1cbk, PDBj:1cbk
PDBsum1cbk
PubMed10080886
UniProtP43777|HPPK_HAEIN 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)

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