Structure of PDB 2o1v Chain B

Receptor sequence
>2o1vB (length=575) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
KLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKI
KCDKEKNLLHVTDTGVGMTREELVKNLGTVGFYSAFLVADKVIVTSKHNN
DTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNL
VKKYSQFINFPIYVWSSKTVWDWELMNDIKPIWQRPSKEVEDDEYKAFYK
SFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAYIKLYVRRVFITDDFHD
MMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKK
IADEKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPSDITSL
DQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDE
YCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAIEKEFEPLLNWMKD
KALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDIS
TNYYASQKKTFEINPRHPLIKDMLRRVKEDEDDKTVSDLAVVLFETATLR
SGYLLPDTKAYGDRIERMLRLSLNI
3D structure
PDB2o1v Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones.
ChainB
Resolution2.45 Å
3D
structure
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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 MG B D737 E740 D563 E566
BS02 ADP B N107 A111 M154 N162 G198 F199 T245 N21 A25 M68 N76 G81 F82 T128 MOAD: 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

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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)

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