Structure of PDB 6ftp Chain A

Receptor sequence
>6ftpA (length=335) Species: 9606 (Homo sapiens) [Search protein sequence]
LASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTE
ILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLS
LLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKD
LDSQTMMVLVNYIFFKAKFEMPFDPQDTHQSRFYLSKKKYVMVPMMSLHH
LTIPYFRDEELSCTVVQLNYTGNASALFILPDQDKMEEVEAMLSQETLSR
FFESLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITG
ARNLAVSQVVHKAVLDVFEEGTERSAATALEVLFQ
3D structure
PDB6ftp Design of an allosterically modulated doxycycline and doxorubicin drug-binding protein.
ChainA
Resolution1.8 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 DM2 A L273 S274 F277 E278 L280 L248 S249 F252 E253 L255 PDBbind-CN: -logKd/Ki=5.82,Kd=1.5uM
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0004867 serine-type endopeptidase inhibitor activity
GO:0005515 protein binding
Biological Process
GO:0006953 acute-phase response
GO:0006954 inflammatory response
GO:0010466 negative regulation of peptidase activity
GO:0019216 regulation of lipid metabolic process
GO:0030277 maintenance of gastrointestinal epithelium
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0031093 platelet alpha granule lumen
GO:0034774 secretory granule lumen
GO:0035578 azurophil granule lumen
GO:0062023 collagen-containing extracellular matrix
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:6ftp, PDBe:6ftp, PDBj:6ftp
PDBsum6ftp
PubMed29760101
UniProtP01011|AACT_HUMAN Alpha-1-antichymotrypsin (Gene Name=SERPINA3)

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