Structure of PDB 5jhy Chain A Binding Site BS01

Receptor Information
>5jhy Chain A (length=735) Species: 242507 (Pyricularia oryzae 70-15) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAE
AFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAM
DGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLML
LTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNN
SVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRM
GMNDTETVALIAGGHAFGKTHGAVKGSNIGPAPEAADLGMQGLGWHNSVG
DGNGPNQMTSGLEVIWTKTPTKWSNGYLESLINNNWTLVESPAGAHQWEA
VNGTVDYPDPFDKTKFRKATMLTSDLALINDPEYLKISQRWLEHPEELAD
AFAKAWFKLLHRDLGPTTRYLGPEVPKESFIWQDPLPAREGDLIDDADVD
KLKAAILSTDGLDVSKLASTAMACATTYRNSDKRGGCNGARIALEPQRNW
VSNNPTQLSAVLDALKKVQSDFNGSNGNKKVSLADLIVLGGTAAVEKAAK
DAGVDIKVPFSAGRVDATQEQTDVTQFSYLEPQADGFRNYGRGTARARTE
EIMVDKASQLTLTPPELTVLVGGMRALGANYDGSDVGVFTANKGKLTPDF
FVNLVDMNIAWTASGADGESWVGTDRKSRSEKYKGSRADLVFGSHAELRA
IAEVYAENGNQEKFVKDFVAAWTKVMNLDRFDLKV
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 chain5jhy Chain A Residue 1500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5jhy Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.
Resolution1.4 Å
Binding residue
(original residue number in PDB)		G133 L134 W140 V274 P276 L309 G313 H314 F316 G317 K318 T319 H320 T358 S359 W365 W455
Binding residue
(residue number reindexed from 1)		G84 L85 W91 V225 P227 L260 G264 H265 F267 G268 K269 T270 H271 T309 S310 W316 W406
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R137 H141 H314 W365 D424
Catalytic site (residue number reindexed from 1) R88 H92 H265 W316 D375
Enzyme Commision number 1.11.1.21: catalase peroxidase.
Gene Ontology
Molecular Function
GO:0004096 catalase activity
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006979 response to oxidative stress
GO:0042744 hydrogen peroxide catabolic process
GO:0070301 cellular response to hydrogen peroxide
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005575 cellular_component
GO:0005576 extracellular region
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5jhy, PDBe:5jhy, PDBj:5jhy
PDBsum5jhy
PubMed27293030
UniProtA4QUT2|KATG2_PYRO7 Catalase-peroxidase 2 (Gene Name=KATG2)

[Back to BioLiP]