Structure of PDB 1hk1 Chain A

Receptor sequence
>1hk1A (length=553) Species: 9606 (Homo sapiens) [Search protein sequence]
SEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCV
ADESAENCDKSLHTLFGDKLCTDCCAKQEPERNECFLQHKDDNPNLPRLV
RPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFT
ECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICE
NQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVC
KNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADP
HECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVP
QVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEK
TPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKET
CFA
3D structure
PDB1hk1 Structural Basis of Albumin-Thyroxine Interactions and Familial Dysalbuminemic Hyperthyroxinemia
ChainA
Resolution2.65 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 T44 A Y150 K199 W214 R218 L219 R222 L238 H242 R257 I290 A291 Y134 K183 W198 R202 L203 R206 L222 H226 R241 I274 A275 PDBbind-CN: -logKd/Ki=5.64,Kd=2.3uM
BS02 T44 A Q390 N391 A406 L407 R410 Y411 L453 S489 Q374 N375 A390 L391 R394 Y395 L437 S473 PDBbind-CN: -logKd/Ki=5.64,Kd=2.3uM
BS03 T44 A F507 T508 I513 K524 K525 A528 F551 A552 F568 F491 T492 I497 K508 K509 A512 F535 A536 F552 PDBbind-CN: -logKd/Ki=5.64,Kd=2.3uM
BS04 T44 A F502 F507 A528 E531 L532 F551 F486 F491 A512 E515 L516 F535 PDBbind-CN: -logKd/Ki=5.64,Kd=2.3uM
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:1hk1, PDBe:1hk1, PDBj:1hk1
PDBsum1hk1
PubMed12743361
UniProtP02768|ALBU_HUMAN Albumin (Gene Name=ALB)

[Back to BioLiP]