Structure of PDB 3koh Chain B Binding Site BS02

Receptor Information

>3koh Chain B (length=463) Species: 9606 (Homo sapiens)

KLPPGPFPLPIIGNLFQLELKNIPKSFTRLAQRFGPVFTLYVGSQRMVVM
HGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGPTWKDIRRFSL
TTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPG
SHRKVIKNVAEVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSA
ERLYTMDGITVTVADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEID
RVIGPSRIPAIKDRQEMPYMDAVVHEIQRFITLVPSNLPHEATRDTIFRG
YLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGKFKYSDYFKPF
STGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS

Ligand information

• Ligand ID: OIO
• InChI: InChI=1S/C11H18N2O2/c14-11(15)6-4-2-1-3-5-8-13-9-7-12-10-13/h7,9-10H,1-6,8H2,(H,14,15)
• InChIKey: OUQGDTNNZRAKIB-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.352: OC(=O)CCCCCCCn1ccnc1
  OpenEye OEToolkits 1.7.0: c1cn(cn1)CCCCCCCC(=O)O
• Formula: C11 H18 N2 O2
• Name: 8-(1H-imidazol-1-yl)octanoic acid
• ChEMBL: CHEMBL1191015
• ZINC: ZINC000038337192
• PDB chain: 3koh Chain B Residue 1

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3koh Human cytochrome P450 2E1 structures with fatty acid analogs reveal a previously unobserved binding mode.
• Resolution: 2.9 Å
• Binding residue (original residue number in PDB): N206 F207 F298 A299 T303
• Binding residue (residue number reindexed from 1): N176 F177 F268 A269 T273
• Annotation score: 2
• Binding affinity: BindingDB: Kd=2.1e+4nM

Enzymatic activity

• Catalytic site (original residue number in PDB): T303 F430 C437
• Catalytic site (residue number reindexed from 1): T273 F400 C407
• Enzyme Commision number: 1.14.13.n7: 4-nitrophenol 2-hydroxylase.
  1.14.14.1: unspecific monooxygenase.

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0005506 iron ion binding
• GO:0008392 arachidonate epoxygenase activity
• GO:0016491 oxidoreductase activity
• GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
• GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
• GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
• GO:0018601 4-nitrophenol 2-monooxygenase activity
• GO:0019825 oxygen binding
• GO:0019899 enzyme binding
• GO:0020037 heme binding
• GO:0030544 Hsp70 protein binding
• GO:0046872 metal ion binding
• GO:0051879 Hsp90 protein binding
• GO:0070330 aromatase activity
• GO:0120319 long-chain fatty acid omega-1 hydroxylase activity

Biological Process

• GO:0001676 long-chain fatty acid metabolic process
• GO:0002933 lipid hydroxylation
• GO:0006631 fatty acid metabolic process
• GO:0006805 xenobiotic metabolic process
• GO:0008202 steroid metabolic process
• GO:0009617 response to bacterium
• GO:0016098 monoterpenoid metabolic process
• GO:0018885 carbon tetrachloride metabolic process
• GO:0018910 benzene metabolic process
• GO:0018960 4-nitrophenol metabolic process
• GO:0019373 epoxygenase P450 pathway
• GO:0042197 halogenated hydrocarbon metabolic process
• GO:0042759 long-chain fatty acid biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005739 mitochondrion
• GO:0005743 mitochondrial inner membrane
• GO:0005783 endoplasmic reticulum
• GO:0005789 endoplasmic reticulum membrane
• GO:0043231 intracellular membrane-bounded organelle

External links

• PDB: RCSB:3koh, PDBe:3koh, PDBj:3koh
• PDBsum: 3koh
• PubMed: 20463018
• UniProt: P05181|CP2E1_HUMAN Cytochrome P450 2E1 (Gene Name=CYP2E1)