Structure of PDB 1llp Chain A Binding Site BS04

Receptor Information
>1llp Chain A (length=343) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATCANGKTVGDASCCAWFDVLDDIQANMFHGGQCGAEAHESIRLVFHDSI
AISPAMEAKGKFGGGGADGSIMIFDTIETAFHPNIGLDEVVAMQKPFVQK
HGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRKPATQPAPDGLVPEPFHT
VDQIIARVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIF
DSQFFVETQFRGTLFPGSGGNQGEVESGMAGEIRIQTDHTLARDSRTACE
WQSFVGNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPLSKPIPGNGP
FSFFPPGKSHSDIEQACAETPFPSLVTLPGPATSVARIPPHKA
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain1llp Chain A Residue 350 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1llp The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		H39 I42 R43 F46 E146 P147 M172 L173 A175 H176 A179 A180 V181 D183 F193
Binding residue
(residue number reindexed from 1)		H39 I42 R43 F46 E146 P147 M172 L173 A175 H176 A179 A180 V181 D183 F193
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1llp, PDBe:1llp, PDBj:1llp
PDBsum1llp
PubMed10024453
UniProtP49012|LIG2_PHACH Ligninase LG2 (Gene Name=GLG2)

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