Structure of PDB 1bke Chain A Binding Site BS02

Receptor Information
>1bke Chain A (length=581) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTC
VADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFL
QHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPE
LLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASL
QKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLEC
ADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLP
SLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTY
ETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKF
QNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYL
SVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFN
AETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAA
FVEKCCKADDKETCFAEEGKKLVAASQAALG
Ligand information
Ligand IDB3I
InChIInChI=1S/C7H3I3O2/c8-3-1-4(7(11)12)6(10)5(9)2-3/h1-2H,(H,11,12)
InChIKeyZMZGFLUUZLELNE-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)c1cc(I)cc(I)c1I
OpenEye OEToolkits 1.5.0c1c(cc(c(c1C(=O)O)I)I)I
ACDLabs 10.04Ic1c(C(=O)O)cc(I)cc1I
FormulaC7 H3 I3 O2
Name2,3,5-TRIIODOBENZOIC ACID
ChEMBLCHEMBL115079
DrugBank
ZINCZINC000003860959
PDB chain1bke Chain A Residue 2002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
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]
PDB1bke Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites.
Resolution3.15 Å
Binding residue
(original residue number in PDB)
H146 Y161 G189 K190
Binding residue
(residue number reindexed from 1)
H143 Y158 G186 K187
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0005504 fatty acid binding
GO:0005507 copper ion binding
GO:0005515 protein binding
GO:0008289 lipid binding
GO:0015643 toxic substance binding
GO:0016209 antioxidant activity
GO:0019825 oxygen binding
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051087 protein-folding chaperone binding
GO:0140272 exogenous protein binding
GO:1903981 enterobactin binding
Biological Process
GO:0009267 cellular response to starvation
GO:0051902 negative regulation of mitochondrial depolarization
GO:0072732 cellular response to calcium ion starvation
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005794 Golgi apparatus
GO:0031093 platelet alpha granule lumen
GO:0032991 protein-containing complex
GO:0070062 extracellular exosome
GO:0072562 blood microparticle

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1bke, PDBe:1bke, PDBj:1bke
PDBsum1bke
PubMed9731778
UniProtP02768|ALBU_HUMAN Albumin (Gene Name=ALB)

[Back to BioLiP]