Structure of PDB 1qpa Chain B Binding Site BS08

Receptor Information
>1qpa Chain B (length=344) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VACPDGVHTASNAACCAWFPVLDDIQQNLFHGGQCGAEAHEALRMVFHDS
IAISPKLQSQGKFGGGGADGSIITFSSIETTYHPNIGLDEVVAIQKPFIA
KHGVTPGDFIAFAGAVGVSNCPGAPQMQFFLGRPEATQAAPDGLVPEPFH
TIDQVLARMLDAGGFDEIETVWLLSAHSIAAANDVDPTISGLPFDSTPGQ
FDSQFFVETQLRGTAFPGKTGIQGTVMSPLKGEMRLQTDHLFARDSRTAC
EWQSFVNNQTKLQEDFQFIFTALSTLGHDMNAMIDCSEVIPAPKPVNFGP
SFFPAGKTHADIEQACASTPFPTLITAPGPSASVARIPPPPSPN
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 chain1qpa Chain B 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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PDB1qpa 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.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		H39 L42 R43 F46 E146 P147 L172 L173 A175 H176 A179 A180 A181 D183 F193 L235
Binding residue
(residue number reindexed from 1)		H40 L43 R44 F47 E147 P148 L173 L174 A176 H177 A180 A181 A182 D184 F194 L236
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H176 F193
Catalytic site (residue number reindexed from 1) H177 F194
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:1qpa, PDBe:1qpa, PDBj:1qpa
PDBsum1qpa
PubMed10024453
UniProtP11542|LIG4_PHACH Ligninase H2 (Gene Name=GLG4)

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