Structure of PDB 4hnp Chain Y Binding Site BS01

Receptor Information
>4hnp Chain Y (length=212) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAA
DCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTM
ICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSV
EDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKV
KEEEGSFNNVIG
Ligand information
Ligand IDVNK
InChIInChI=1S/C27H52N4O5/c1-10-11-12-13-22(32)30-24(18(4)5)27(36)28-20(14-15-23(33)31(8)9)26(35)29-21(16-17(2)3)25(34)19(6)7/h17-21,24-25,34H,10-16H2,1-9H3,(H,28,36)(H,29,35)(H,30,32)/t20-,21-,24-,25-/m0/s1
InChIKeyNHNWMUWCUHYJIR-NBMBROAQSA-N
SMILES
SoftwareSMILES
CACTVS 3.370CCCCCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)N(C)C)C(=O)N[C@@H](CC(C)C)[C@@H](O)C(C)C
OpenEye OEToolkits 1.7.6CCCCCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)N(C)C)C(=O)N[C@@H](CC(C)C)[C@H](C(C)C)O
CACTVS 3.370CCCCCC(=O)N[CH](C(C)C)C(=O)N[CH](CCC(=O)N(C)C)C(=O)N[CH](CC(C)C)[CH](O)C(C)C
OpenEye OEToolkits 1.7.6CCCCCC(=O)NC(C(C)C)C(=O)NC(CCC(=O)N(C)C)C(=O)NC(CC(C)C)C(C(C)C)O
ACDLabs 12.01O=C(NC(CC(C)C)C(O)C(C)C)C(NC(=O)C(NC(=O)CCCCC)C(C)C)CCC(=O)N(C)C
FormulaC27 H52 N4 O5
NameN-hexanoyl-L-valyl-N~1~-[(3S,4S)-3-hydroxy-2,6-dimethylheptan-4-yl]-N~5~,N~5~-dimethyl-L-glutamamide;
vinylketone carmaphycin analogue VNK1, double bound form
ChEMBL
DrugBank
ZINCZINC000098209530
PDB chain4hnp Chain Y Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4hnp Enzyme inhibition by hydroamination: design and mechanism of a hybrid carmaphycin-syringolin enone proteasome inhibitor.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		T1 A20 T21 G47 A49
Binding residue
(residue number reindexed from 1)		T1 A20 T21 G47 A49
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T1 D17 R19 K33 G47 S131 D168 S171
Catalytic site (residue number reindexed from 1) T1 D17 R19 K33 G47 S131 D168 S171
Enzyme Commision number 3.4.25.1: proteasome endopeptidase complex.
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
Biological Process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005839 proteasome core complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4hnp, PDBe:4hnp, PDBj:4hnp
PDBsum4hnp
PubMed24930969
UniProtP30656|PSB5_YEAST Proteasome subunit beta type-5 (Gene Name=PRE2)

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