Structure of PDB 6ftp Chain A Binding Site BS01

Receptor Information
>6ftp Chain A (length=335) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTE
ILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLS
LLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKD
LDSQTMMVLVNYIFFKAKFEMPFDPQDTHQSRFYLSKKKYVMVPMMSLHH
LTIPYFRDEELSCTVVQLNYTGNASALFILPDQDKMEEVEAMLSQETLSR
FFESLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITG
ARNLAVSQVVHKAVLDVFEEGTERSAATALEVLFQ
Ligand information
Ligand IDDM2
InChIInChI=1S/C27H29NO11/c1-10-22(31)13(28)6-17(38-10)39-15-8-27(36,16(30)9-29)7-12-19(15)26(35)21-20(24(12)33)23(32)11-4-3-5-14(37-2)18(11)25(21)34/h3-5,10,13,15,17,22,29,31,33,35-36H,6-9,28H2,1-2H3/t10-,13-,15-,17-,22+,27-/m0/s1
InChIKeyAOJJSUZBOXZQNB-TZSSRYMLSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COc1cccc2C(=O)c3c(O)c4C[C@](O)(C[C@H](O[C@H]5C[C@H](N)[C@H](O)[C@H](C)O5)c4c(O)c3C(=O)c12)C(=O)CO
OpenEye OEToolkits 1.5.0CC1C(C(CC(O1)OC2CC(Cc3c2c(c4c(c3O)C(=O)c5cccc(c5C4=O)OC)O)(C(=O)CO)O)N)O
ACDLabs 10.04O=C2c1c(O)c5c(c(O)c1C(=O)c3cccc(OC)c23)CC(O)(C(=O)CO)CC5OC4OC(C(O)C(N)C4)C
OpenEye OEToolkits 1.5.0C[C@H]1[C@H]([C@H](C[C@@H](O1)O[C@H]2C[C@@](Cc3c2c(c4c(c3O)C(=O)c5cccc(c5C4=O)OC)O)(C(=O)CO)O)N)O
CACTVS 3.341COc1cccc2C(=O)c3c(O)c4C[C](O)(C[CH](O[CH]5C[CH](N)[CH](O)[CH](C)O5)c4c(O)c3C(=O)c12)C(=O)CO
FormulaC27 H29 N O11
NameDOXORUBICIN;
ADRIAMYCIN
ChEMBLCHEMBL53463
DrugBankDB00997
ZINCZINC000003918087
PDB chain6ftp Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6ftp Design of an allosterically modulated doxycycline and doxorubicin drug-binding protein.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		L273 S274 F277 E278 L280
Binding residue
(residue number reindexed from 1)		L248 S249 F252 E253 L255
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=5.82,Kd=1.5uM
Enzymatic activity
Enzyme Commision number ?
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
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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