Structure of PDB 1b85 Chain A Binding Site BS03

Receptor Information
>1b85 Chain A (length=348) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IEKRATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLVF
HDSIAISPAMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQKP
FVQKHGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRAPATQPAPDGLVPE
PFHTVDQIINRVNDAGEFDELELVFMLSAHSVAAVNDVDPTVQGLPFDST
PGIFDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDHTIARDSR
TACEWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQSKPIP
GNLPFSFFPAGKTIKDVEQACAETPFPTLTTLPGPETSVQRIPPPPGA
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 chain1b85 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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PDB1b85 Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.
Resolution1.85 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)		H43 I46 R47 F50 E150 P151 M176 L177 A179 H180 A183 A184 V185 D187 F197
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R43 H47 H176 F193 D238
Catalytic site (residue number reindexed from 1) R47 H51 H180 F197 D242
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:1b85, PDBe:1b85, PDBj:1b85
PDBsum1b85
PubMed11162097
UniProtP06181|LIG8_PHACH Ligninase H8 (Gene Name=LPOA)

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