Structure of PDB 4ntm Chain F Binding Site BS02

Receptor Information
>4ntm Chain F (length=118) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTLFKDFTFEAAHRLPHVPEGHKCGRLHGHSFMVRLEITGEVDPHTGWII
DFAELKAAFKPTYERLDHHYLNDIPGLENPTSEVLAKWIWDQVKPVVPLL
SAVMVKETCTAGCIYRGE
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4ntm Chain F Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4ntm Biochemical and Structural Studies of 6-Carboxy-5,6,7,8-tetrahydropterin Synthase Reveal the Molecular Basis of Catalytic Promiscuity within the Tunnel-fold Superfamily.
Resolution2.05 Å
Binding residue
(original residue number in PDB)		H16 H31 H33
Binding residue
(residue number reindexed from 1)		H13 H28 H30
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C27 H31 H33 E110
Catalytic site (residue number reindexed from 1) C24 H28 H30 E107
Enzyme Commision number 4.1.2.50: 6-carboxytetrahydropterin synthase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0070497 6-carboxy-5,6,7,8-tetrahydropterin synthase activity
Biological Process
GO:0008616 queuosine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4ntm, PDBe:4ntm, PDBj:4ntm
PDBsum4ntm
PubMed24990950
UniProtP65870|QUED_ECOLI 6-carboxy-5,6,7,8-tetrahydropterin synthase (Gene Name=queD)

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