Structure of PDB 1lga Chain B Binding Site BS02

Receptor Information
>1lga Chain B (length=341) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATCANGKTVGDASCCAWFDVLDDIQANMFHGGQCGAEAHESIRLVFHDSI
AISPAMEAKGKFGGGGADGSIMIFDTIETAFHPNIGLDEVVAMQKPFVQK
HGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRKPATQPAPDGLVPEPFHT
VDQIIARVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIF
DSQFFVETQFRGTLFPGSGGNQGEVESGMAGEIRIQTDHTLARDSRTACE
WQSFVGNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPLSKPIPGNGP
FSFFPPGKSHSDIEQACAETPFPSLVTLPGPATSVARIPPH
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1lga Chain B Residue 399 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lga Crystallographic refinement of lignin peroxidase at 2 A.
Resolution2.03 Å
Binding residue
(original residue number in PDB)		D48 G66 D68 S70
Binding residue
(residue number reindexed from 1)		D48 G66 D68 S70
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H176 F193
Catalytic site (residue number reindexed from 1) H176 F193
Enzyme Commision number 1.11.1.14: lignin peroxidase.
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016690 diarylpropane peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0000302 response to reactive oxygen species
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress
GO:0042744 hydrogen peroxide catabolic process
GO:0046274 lignin catabolic process
GO:0098869 cellular oxidant detoxification

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Molecular Function
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Biological Process
External links
PDB RCSB:1lga, PDBe:1lga, PDBj:1lga
PDBsum1lga
PubMed8440725
UniProtP49012|LIG2_PHACH Ligninase LG2 (Gene Name=GLG2)

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