Structure of PDB 2o1v Chain A

Receptor sequence
>2o1vA (length=578) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
MMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTV
KIKCDKEKNLLHVTDTGVGMTREELVKNLGTVGFYSAFLVADKVIVTSKH
NNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIK
NLVKKYSQFINFPIYVWSSKVWDWELMNDIKPIWQRPSKEVEDDEYKAFY
KSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRYIKLYVRRVFITDD
FHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDM
IKKIADEKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPSDI
TSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEP
VDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAIEKEFEPLLNW
MKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGK
DISTNYYASQKKTFEINPRHPLIKDMLRRVKEDEDDKTVSDLAVVLFETA
TLRSGYLLPDTKAYGDRIERMLRLSLNI
3D structure
PDB2o1v Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones.
ChainA
Resolution2.45 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ADP A N107 A111 D149 M154 N162 G198 F199 N23 A27 D65 M70 N78 G83 F84 MOAD: Kd~5uM
PDBbind-CN: -logKd/Ki=5.30,Kd=5uM
BindingDB: IC50=11447nM,EC50=21000nM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2o1v, PDBe:2o1v, PDBj:2o1v
PDBsum2o1v
PubMed17936703
UniProtP41148|ENPL_CANLF Endoplasmin (Gene Name=HSP90B1)

[Back to BioLiP]