Structure of PDB 4v4o Chain A Binding Site BS01

Receptor Information
>4v4o Chain A (length=527) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKILVFDEAARRALERGVNAVANAVKVTLGPRGRNVVLEKKFGSPTITKD
GVTVAKEVELEDHLENIGAQLLKEVASKTNDVAGDGTTTATVLAQAIVRE
GLKNVAAGANPLALKRGIEKAVEAAVEKIKALAIPVEDRKAIEEVATISA
NDPEVGKLIADAMEKVGKEGIITVEESKSLETELKFVEGYQFDKGYISPY
FVTNPETMEAVLEDAFILIVEKKVSNVRELLPILEQVAQTGKPLLIIAED
VEGEALATLVVNKLRGTLSVAAVKAPGFGDRRKEMLKDIAAVTGGTVISE
ELGFKLENATLSMLGRAERVRITKDETTIVGGKGKKEDIEARINGIKKEL
ETTDSEYAREKLQERLAKLAGGVAVIRVGAATETELKEKKHRFEDALNAT
RAAVEEGIVPGGGVTLLRAISAVEELIKKLEGDEATGAKIVRRALEEPAR
QIAENAGYEGSVIVQQILAETKNPRYGFNAATGEFVDMVEAGIVDPAKVT
RSALQNAASIGALILTTEAVVAEKPEK
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain4v4o Chain A Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4v4o Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
Resolution2.8 Å
Binding residue
(original residue number in PDB)		G32 P33 K51 D87 G88 T90 T91 I150 G414 A482 I495 D497
Binding residue
(residue number reindexed from 1)		G30 P31 K49 D85 G86 T88 T89 I148 G412 A480 I493 D495
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D52 T89 T90 D397
Catalytic site (residue number reindexed from 1) D50 T87 T88 D395
Enzyme Commision number 5.6.1.7: chaperonin ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016853 isomerase activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0009408 response to heat
GO:0042026 protein refolding
GO:0051085 chaperone cofactor-dependent protein refolding
Cellular Component
GO:0005737 cytoplasm
GO:1990220 GroEL-GroES complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4v4o, PDBe:4v4o, PDBj:4v4o
PDBsum4v4o
PubMed15296740
UniProtP61490|CH60_THET2 Chaperonin GroEL (Gene Name=groEL)

[Back to BioLiP]