Structure of PDB 5abq Chain A Binding Site BS01

Receptor Information
>5abq Chain A (length=312) Species: 5323 (Pleurotus eryngii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDCIGF
SPTLGGGGCDGSIIAFSDIETNFPANAGIDEIVEAQKPFVAKHNISAGDF
IQFAGAVGVSNCPGGVRIPFFLGRPDAVKASPDHLVPEPFDSVTSILARM
GDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETL
LKGRLFPGTADNKGEAQSPLQGEIRLQSDELLARDPRTACEWQSMVNNQP
KIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLKD
VEQACRKTPFPR
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 chain5abq Chain A Residue 500 [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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PDB5abq Improving the Ph-Stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase.
Resolution2.293 Å
Binding residue
(original residue number in PDB)		H39 L42 R43 F46 P139 E140 P141 L166 S168 H169 A172 A173 A174 D175 K176 F186 L228
Binding residue
(residue number reindexed from 1)		H37 L40 R41 F44 P137 E138 P139 L164 S166 H167 A170 A171 A172 D173 K174 F184 L226
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R43 H47 H169 F186 D231
Catalytic site (residue number reindexed from 1) R41 H45 H167 F184 D229
Enzyme Commision number 1.11.1.16: versatile peroxidase.
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016689 manganese peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0052750 reactive-black-5:hydrogen-peroxide oxidoreductase activity
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
Cellular Component
GO:0005576 extracellular region

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Biological Process
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Cellular Component
External links
PDB RCSB:5abq, PDBe:5abq, PDBj:5abq
PDBsum5abq
PubMed26496708
UniProtO94753|VPL2_PLEER Versatile peroxidase VPL2 (Gene Name=vpl2)

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