Structure of PDB 3d2o Chain A

Receptor sequence
>3d2oA (length=244) Species: 485 (Neisseria gonorrhoeae) [Search protein sequence]
RNLPINQVGIKDLRFPITLKTAEGTQSTVARLTMTVYLPAEQKGTHMSRF
VALMEQHTEVLDFAQLHRLTAEMVALLDSRAGKISVSFPFFRKKTAPVSG
IRSLLDYDVSLTGEMKDGAYGHSMKVMIPVTSLCPCSKEISQYGAHNQRS
HVTVSLTSDAEVGIEEVIDYVETQASCQLYGLLKRPDEKYVTEKAYENPK
FVEDMVRDVATSLIADKRIKSFVVESENFESIHNHSAYAYIAYP
3D structure
PDB3d2o Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence for GTP cyclohydrolase IB
ChainA
Resolution2.04 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.4.16: GTP cyclohydrolase I.
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 C147 H159 C134 H146
Gene Ontology
Molecular Function
GO:0003933 GTP cyclohydrolase activity
GO:0003934 GTP cyclohydrolase I activity
GO:0016787 hydrolase activity
Biological Process
GO:0046654 tetrahydrofolate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3d2o, PDBe:3d2o, PDBj:3d2o
PDBsum3d2o
PubMed19767425
UniProtQ5F9K6|GCH4_NEIG1 GTP cyclohydrolase FolE2 (Gene Name=folE2)

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