Structure of PDB 3od4 Chain A Binding Site BS02

Receptor Information
>3od4 Chain A (length=342) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIE
NEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKK
MANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRK
IVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFF
AQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQN
VVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIE
YPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN
Ligand information
Ligand ID8XQ
InChIInChI=1S/C10H7NO3/c12-8-4-3-7(10(13)14)6-2-1-5-11-9(6)8/h1-5,12H,(H,13,14)
InChIKeyJGRPKOGHYBAVMW-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)c1ccc(O)c2ncccc12
CACTVS 3.370OC(=O)c1ccc(O)c2ncccc12
OpenEye OEToolkits 1.7.0c1cc2c(ccc(c2nc1)O)C(=O)O
FormulaC10 H7 N O3
Name8-hydroxyquinoline-5-carboxylic acid
ChEMBLCHEMBL1230640
DrugBank
ZINCZINC000005933707
PDB chain3od4 Chain A Residue 350 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3od4 Crystal Structure of Factor Inhibiting HIF-1 Alpha Complexed with Inhibitor
Resolution2.2 Å
Binding residue
(original residue number in PDB)		Y145 L188 T196 H199 F207 K214 H279 I281 N294
Binding residue
(residue number reindexed from 1)		Y138 L181 T189 H192 F200 K207 H272 I274 N287
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.11.30: hypoxia-inducible factor-asparagine dioxygenase.
1.14.11.n4: ankyrin-repeat-histidine dioxagenase.
Gene Ontology
Molecular Function
GO:0003714 transcription corepressor activity
GO:0005112 Notch binding
GO:0005515 protein binding
GO:0008198 ferrous iron binding
GO:0008270 zinc ion binding
GO:0019826 oxygen sensor activity
GO:0031406 carboxylic acid binding
GO:0036139 peptidyl-histidine dioxygenase activity
GO:0036140 [protein]-asparagine 3-dioxygenase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0051059 NF-kappaB binding
GO:0051213 dioxygenase activity
GO:0062101 peptidyl-aspartic acid 3-dioxygenase activity
GO:0071532 ankyrin repeat binding
Biological Process
GO:0045663 positive regulation of myoblast differentiation
GO:0045746 negative regulation of Notch signaling pathway
GO:0045892 negative regulation of DNA-templated transcription
GO:2001214 positive regulation of vasculogenesis
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0048471 perinuclear region of cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3od4, PDBe:3od4, PDBj:3od4
PDBsum3od4
PubMed
UniProtQ9NWT6|HIF1N_HUMAN Hypoxia-inducible factor 1-alpha inhibitor (Gene Name=HIF1AN)

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