Structure of PDB 2o1u Chain B

Receptor sequence
>2o1uB (length=575) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
KLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKI
KCDKEKNLLHVTDTGVGMTREELVKNLGTVGFYSAFLVADKVIVTSKHNN
DTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNL
VKKYSQFINFPIYVWSSKTVWDWELMNDIKPIWQRPSKEVEDDEYKAFYK
SFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAYIKLYVRRVFITDDFHD
MMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKK
IADEKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPSDITSL
DQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDE
YCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAIEKEFEPLLNWMKD
KALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDIS
TNYYASQKKTFEINPRHPLIKDMLRRVKEDEDDKTVSDLAVVLFETATLR
SGYLLPDTKAYGDRIERMLRLSLNI
3D structure
PDB2o1u Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones.
ChainB
Resolution2.4 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 E103 N107 E17 N21
BS02 ANP B N107 A111 M154 G198 F199 T245 N21 A25 M68 G81 F82 T128
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:2o1u, PDBe:2o1u, PDBj:2o1u
PDBsum2o1u
PubMed17936703
UniProtP41148|ENPL_CANLF Endoplasmin (Gene Name=HSP90B1)

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