Structure of PDB 3d2o Chain B Binding Site BS01

Receptor Information
>3d2o Chain B (length=243) Species: 485 (Neisseria gonorrhoeae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLPINQVGIKDLRFPITLKTAEGTQSTVARLTMTVYLPAEQKGTHMSRFV
ALMEQHTEVLDFAQLHRLTAEMVALLDSRAGKISVSFPFFRKKTAPVSGI
RSLLDYDVSLTGEMKDGAYGHSMKVMIPVTSLCPCSKEISQYGAHNQRSH
VTVSLTSDAEVGIEEVIDYVETQASCQLYGLLKRPDEKYVTEKAYENPKF
VEDMVRDVATSLIADKRIKSFVVESENFESIHNHSAYAYIAYP
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain3d2o Chain B Residue 258 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3d2o Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence for GTP cyclohydrolase IB
Resolution2.04 Å
Binding residue
(original residue number in PDB)		C147 H159
Binding residue
(residue number reindexed from 1)		C133 H145
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.4.16: GTP cyclohydrolase I.
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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