Structure of PDB 1fha Chain A Binding Site BS01
Receptor Information
>1fha Chain A (length=172) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKY
FLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDCDDWESGLNAMECAL
HLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTN
LRKMGAPESGLAEYLFDKHTLG
Ligand information
Ligand ID
FE
InChI
InChI=1S/Fe/q+3
InChIKey
VTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
Formula
Fe
Name
FE (III) ION
ChEMBL
DrugBank
DB13949
ZINC
PDB chain
1fha Chain A Residue 200 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure 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
]
PDB
1fha
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts.
Resolution
2.4 Å
Binding residue
(original residue number in PDB)
E27 E62 H65
Binding residue
(residue number reindexed from 1)
E23 E58 H61
Annotation score
5
Enzymatic activity
Enzyme Commision number
1.16.3.1
: ferroxidase.
Gene Ontology
Molecular Function
GO:0004322
ferroxidase activity
GO:0005506
iron ion binding
GO:0005515
protein binding
GO:0008198
ferrous iron binding
GO:0008199
ferric iron binding
GO:0016491
oxidoreductase activity
GO:0042802
identical protein binding
GO:0046872
metal ion binding
GO:0140315
iron ion sequestering activity
Biological Process
GO:0006826
iron ion transport
GO:0006879
intracellular iron ion homeostasis
GO:0006880
intracellular sequestering of iron ion
GO:0006955
immune response
GO:0008285
negative regulation of cell population proliferation
GO:0048147
negative regulation of fibroblast proliferation
GO:0110076
negative regulation of ferroptosis
Cellular Component
GO:0005576
extracellular region
GO:0005634
nucleus
GO:0005737
cytoplasm
GO:0005764
lysosome
GO:0005776
autophagosome
GO:0005829
cytosol
GO:0016020
membrane
GO:0031410
cytoplasmic vesicle
GO:0044754
autolysosome
GO:0070062
extracellular exosome
GO:0070288
ferritin complex
GO:1904724
tertiary granule lumen
GO:1904813
ficolin-1-rich granule lumen
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1fha
,
PDBe:1fha
,
PDBj:1fha
PDBsum
1fha
PubMed
1992356
UniProt
P02794
|FRIH_HUMAN Ferritin heavy chain (Gene Name=FTH1)
[
Back to BioLiP
]