Structure of PDB 2bxq Chain A

Receptor sequence
>2bxqA (length=582) Species: 9606 (Homo sapiens) [Search protein sequence]
HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKT
CVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECF
LQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAP
ELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCAS
LQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLE
CADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADL
PSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKT
YETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDY
LSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEF
NAETFTFHADICTLSEKEEQIKKQTALVELVKHKPKATKEQLKAVMDDFA
AFVEKCCKADDKETCFAEEGKKLVAASQAALG
3D structure
PDB2bxq Structural Basis of the Drug-Binding Specificity of Human Serum Albumin.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 IMN A K199 S202 A210 F211 W214 A215 R218 L238 K197 S200 A208 F209 W212 A213 R216 L236 BindingDB: Kd=700nM,Ki=15135612484362nM
BS02 P1Z A K199 L219 R222 F223 L238 H242 R257 L260 S287 I290 A291 K197 L217 R220 F221 L236 H240 R255 L258 S285 I288 A289
BS03 IMN A R114 L115 H146 F157 R186 G189 K190 R112 L113 H144 F155 R184 G187 K188 BindingDB: Kd=700nM,Ki=15135612484362nM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2bxq, PDBe:2bxq, PDBj:2bxq
PDBsum2bxq
PubMed16169013
UniProtP02768|ALBU_HUMAN Albumin (Gene Name=ALB)

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