Structure of PDB 4hhr Chain A Binding Site BS01

Receptor Information

>4hhr Chain A (length=640) Species: 3702 (Arabidopsis thaliana)

SMKVITSLISSILLKFIHKDFHEIYARMSLLDRFLLLIVHGVDKMVPWHK
LPVFLGLTYLEVRRHLHQQYNLLNVGQTPTGIRFDPANYPYRTADGKFND
PFNEGVGSQNSFFGRNCPPVDQKSKLRRPDPMVVATKLLGRKKFIDTGKQ
FNMIAASWIQFMIHDWIDHLEDTHQIELVAPKEVASKCPLSSFRFLKTKE
VPTGFFEIKTGSQNIRTPWWDSSVIYGSNSKTLDRVRTYKDGKLKISEET
GLLLHDEDGLAISGDIRNSWAGVSALQALFIKEHNAVCDALKDEDDDLED
EDLYRYARLVTSAVVAKIHTIDWTVQLLKTDTLLAGMRANWYGLLGKKFK
DSFGHAGSSILGGVVGMKKPQNHGVPYSLTEDFTSVYRMHSLLPDQLHIL
DIDDVPGTNKSLPLIQEISMRDLIGRKGEETMSHIGFTKLMVSMGHQASG
ALELMNYPMWLRDIVPHDPNGQARPDHVDLAALEIYRDRERSVPRYNEFR
RSMFMIPITKWEDLTEDEEAIEVLDDVYDGDVEELDLLVGLMAEKKIKGF
AISETAFYIFLIMATRRLEADRFFTSDFNETIYTKKGLEWVNTTESLKDV
IDRHYPDMTDKWMNSESAFSVWDSPPLTKNPIPLYLRIPS

Ligand information

• Ligand ID: HEM
• InChI: InChI=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-;
• InChIKey: KABFMIBPWCXCRK-RGGAHWMASA-L
• SMILES:
  OpenEye OEToolkits 1.7.6: Cc1c2n3c(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 3.385: CC1=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 12.01: C=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
• Formula: C34 H32 Fe N4 O4
• Name: PROTOPORPHYRIN IX CONTAINING FE;
  HEME
• DrugBank: DB18267
• PDB chain: 4hhr Chain A Residue 701

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4hhr The crystal structure of alpha-Dioxygenase provides insight into diversity in the cyclooxygenase-peroxidase superfamily.
• Resolution: 1.51 Å
• Binding residue (original residue number in PDB): I158 Q159 D167 H168 N267 W269 T383 Y386 M388 H389 L392 L479 L482 R486 R490
• Binding residue (residue number reindexed from 1): I159 Q160 D168 H169 N268 W270 T384 Y387 M389 H390 L393 L480 L483 R487 R491
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Q159 H163
• Catalytic site (residue number reindexed from 1): Q160 H164
• Enzyme Commision number: 1.13.11.92: fatty acid alpha-dioxygenase.

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0016491 oxidoreductase activity
• GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
• GO:0020037 heme binding
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity

Biological Process

• GO:0001561 fatty acid alpha-oxidation
• GO:0006629 lipid metabolic process
• GO:0006631 fatty acid metabolic process
• GO:0006633 fatty acid biosynthetic process
• GO:0006979 response to oxidative stress
• GO:0008219 cell death
• GO:0009626 plant-type hypersensitive response
• GO:0009627 systemic acquired resistance
• GO:0009737 response to abscisic acid
• GO:0009751 response to salicylic acid
• GO:0031408 oxylipin biosynthetic process
• GO:0034614 cellular response to reactive oxygen species
• GO:0042742 defense response to bacterium
• GO:0050832 defense response to fungus
• GO:0071446 cellular response to salicylic acid stimulus
• GO:0071732 cellular response to nitric oxide
• GO:0098869 cellular oxidant detoxification
• GO:1902609 (R)-2-hydroxy-alpha-linolenic acid biosynthetic process

Cellular Component

• GO:0005811 lipid droplet
• GO:0012511 monolayer-surrounded lipid storage body

External links

• PDB: RCSB:4hhr, PDBe:4hhr, PDBj:4hhr
• PDBsum: 4hhr
• PubMed: 23373518
• UniProt: Q9SGH6|DOX1_ARATH Alpha-dioxygenase 1 (Gene Name=DOX1)