Structure of PDB 1x6m Chain D Binding Site BS01

Receptor Information
>1x6m Chain D (length=194) Species: 266 (Paracoccus denitrificans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVDTSGVKIHPAVDNGIKPAQPGFAGGTLHCKCSTNPVRVAVRAQTAHNH
VCGCTKCWKPEGAIFSQVAVVGRDALEVLEGAEKLEIVNAEAPIQRHRCR
DCGVHMYGRIENRDHPFYGLDFVHTELSDEDGWSAPEFAAFVSSIIESGV
DPSRMEAIRARLRELGLEPYDALSPPLMDAIATHIAKRSGALAA
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 chain1x6m Chain D Residue 200 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1x6m A dynamic zinc redox switch
Resolution2.35 Å
Binding residue
(original residue number in PDB)
C33 C35 C101 C104
Binding residue
(residue number reindexed from 1)
C31 C33 C99 C102
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C54 C56 C59
Catalytic site (residue number reindexed from 1) C52 C54 C57
Enzyme Commision number 4.4.1.22: S-(hydroxymethyl)glutathione synthase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016846 carbon-sulfur lyase activity
GO:0046872 metal ion binding
GO:0051907 S-(hydroxymethyl)glutathione synthase activity
Biological Process
GO:0046294 formaldehyde catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1x6m, PDBe:1x6m, PDBj:1x6m
PDBsum1x6m
PubMed15548539
UniProtQ51669|GFA_PARDE Glutathione-dependent formaldehyde-activating enzyme (Gene Name=gfa)

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