Structure of PDB 4ntm Chain E

Receptor sequence
>4ntmE (length=118) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
STTLFKDFTFEAAHRLPHVPEGHKCGRLHGHSFMVRLEITGEVDPHTGWI
IDFAELKAAFKPTYERLDHHYLNDIPGLENPTSEVLAKWIWDQVKPVVPL
LSAVMVKETCTAGCIYRG
3D structure
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.
ChainE
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C27 H31 H33 E110
Catalytic site (residue number reindexed from 1) C25 H29 H31 E108
Enzyme Commision number 4.1.2.50: 6-carboxytetrahydropterin synthase.
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 2K8 E W51 F55 W49 F53
BS02 ZN E H16 H31 H33 H14 H29 H31
BS03 2K8 E H16 C27 T84 S85 E86 E110 H14 C25 T82 S83 E84 E108
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
View graph for
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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