Structure of PDB 1h2l Chain A Binding Site BS01

Receptor Information
>1h2l Chain A (length=332) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVL
TDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNF
KPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLG
FNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYK
RCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETV
VGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPEYPLKAHQKVA
IMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN
Ligand information
>1h2l Chain S (length=22) Species: 9606 (Homo sapiens) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
LTSYDCEVNAPILQGEELLRAL
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]
PDB1h2l Structure of Factor-Inhibiting Hypoxia-Inducible Factor (Hif) Reveals Mechanism of Oxidative Modification of Hif-1Alpha
Resolution2.25 Å
Binding residue
(original residue number in PDB)		Y102 T149 N151 D152 F162 W167 Q181 L182 T183 S184 H199 D201 E202 Q203 R238 Q239 M275 Y276 W296 G299 A300 T302 N321
Binding residue
(residue number reindexed from 1)		Y88 T135 N137 D138 F148 W153 Q167 L168 T169 S170 H185 D187 E188 Q189 R224 Q225 M261 Y262 W282 G285 A286 T288 N304
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1h2l, PDBe:1h2l, PDBj:1h2l
PDBsum1h2l
PubMed12446723
UniProtQ9NWT6|HIF1N_HUMAN Hypoxia-inducible factor 1-alpha inhibitor (Gene Name=HIF1AN)

[Back to BioLiP]