Structure of PDB 5fpn Chain A Binding Site BS01

Receptor Information
>5fpn Chain A (length=379) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGD
AAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKV
QVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDS
QRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCGEKNVLIFDLGGG
TFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDI
GPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFE
ELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDF
FNGKELNKSINPDEAVAYGAAVQAAILIG
Ligand information
Ligand IDKYD
InChIInChI=1S/C6H8N2O2/c1-3-5(6(9)10)4(2)8-7-3/h1-2H3,(H,7,8)(H,9,10)
InChIKeyIOOWDXMXZBYKLR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c(c(n[nH]1)C)C(=O)O
CACTVS 3.385Cc1[nH]nc(C)c1C(O)=O
FormulaC6 H8 N2 O2
Name3,5-DIMETHYL-1H-PYRAZOLE-4-CARBOXYLIC ACID
ChEMBL
DrugBank
ZINCZINC000000158520
PDB chain5fpn Chain A Residue 1385 [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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PDB5fpn Detection of Secondary Binding Sites in Proteins Using Fragment Screening.
Resolution1.96 Å
Binding residue
(original residue number in PDB)		R49 S121 M122 T125
Binding residue
(residue number reindexed from 1)		R46 S118 M119 T122
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D10 K71 E175 D201
Catalytic site (residue number reindexed from 1) D7 K68 E172 D196
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0019899 enzyme binding
GO:0031072 heat shock protein binding
GO:0044183 protein folding chaperone
GO:0048156 tau protein binding
GO:0051082 unfolded protein binding
GO:0051087 protein-folding chaperone binding
GO:0051861 glycolipid binding
GO:0097718 disordered domain specific binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006986 response to unfolded protein
GO:0007140 male meiotic nuclear division
GO:0007141 male meiosis I
GO:0007283 spermatogenesis
GO:0007286 spermatid development
GO:0009408 response to heat
GO:0009409 response to cold
GO:0010971 positive regulation of G2/M transition of mitotic cell cycle
GO:0030154 cell differentiation
GO:0032781 positive regulation of ATP-dependent activity
GO:0042026 protein refolding
GO:0051085 chaperone cofactor-dependent protein refolding
GO:0070194 synaptonemal complex disassembly
GO:0090084 negative regulation of inclusion body assembly
GO:1901896 positive regulation of ATPase-coupled calcium transmembrane transporter activity
Cellular Component
GO:0000795 synaptonemal complex
GO:0001673 male germ cell nucleus
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005819 spindle
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0036128 CatSper complex
GO:0070062 extracellular exosome
GO:0072562 blood microparticle
GO:0072687 meiotic spindle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fpn, PDBe:5fpn, PDBj:5fpn
PDBsum5fpn
PubMed26655740
UniProtP54652|HSP72_HUMAN Heat shock-related 70 kDa protein 2 (Gene Name=HSPA2)

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