Structure of PDB 2o1u Chain A

Receptor sequence
>2o1uA (length=578) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
MMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTV
KIKCDKEKNLLHVTDTGVGMTREELVKNLGTVGFYSAFLVADKVIVTSKH
NNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIK
NLVKKYSQFINFPIYVWSSKVWDWELMNDIKPIWQRPSKEVEDDEYKAFY
KSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRYIKLYVRRVFITDD
FHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDM
IKKIADEKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPSDI
TSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEP
VDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAIEKEFEPLLNW
MKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGK
DISTNYYASQKKTFEINPRHPLIKDMLRRVKEDEDDKTVSDLAVVLFETA
TLRSGYLLPDTKAYGDRIERMLRLSLNI
3D structure
PDB2o1u Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones.
ChainA
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 A D737 E740 D566 E569
BS02 ANP A N107 M154 N162 G198 F199 N23 M70 N78 G83 F84
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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