Structure of PDB 1zyk Chain C Binding Site BS01

Receptor Information
>1zyk Chain C (length=343) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNINEILKKLINKSDLEINEAEELAKAIIRGEVPEILVSAILVALRMKGE
SKNEIVGFARAMRELAIKIDVPNAIDTAGTGGDGLGTVNVSTASAILLSL
VNPVAKHGNRAVSGKSGSADVLEALGYNIIVPPERAKELVNKTNFVFLFA
QYYHPAMKNVANVRKTLGIRTIFNILGPLTNPANAKYQLMGVFSKDHLDL
LSKSAYELDFNKIILVYGEPGIDEVSPIGNTFMKIVSKRGIEEVKLNVTD
FGISPIPIEKLIVNSAEDSAIKIVRAFLGKDEHVAEFIKINTAVALFALD
RVGDFREGYEYADHLIEKSLDKLNEIISMNGDVTKLKTIVVKS
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1zyk Chain C Residue 706 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1zyk Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.
Resolution2.4 Å
Binding residue
(original residue number in PDB)
D223 E224
Binding residue
(residue number reindexed from 1)
D223 E224
Annotation score1
Enzymatic activity
Enzyme Commision number 2.4.2.18: anthranilate phosphoribosyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004048 anthranilate phosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000162 tryptophan biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1zyk, PDBe:1zyk, PDBj:1zyk
PDBsum1zyk
PubMed16714288
UniProtP50384|TRPD_SACS2 Anthranilate phosphoribosyltransferase (Gene Name=trpD)

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