7S65

Compressed conformation of nighttime state KaiC


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Hidden conformations differentiate day and night in a circadian pacemaker

Swan, J.A.Sandate, C.R.Chavan, A.G.Freeberg, A.M.Etwaru, D.Palacios, J.G.Golden, S.S.Liwang, A.Lander, G.C.Partch, C.L.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
Circadian clock protein kinase KaiC
A, B, C, D, E, F
A, B, C, D, E, F
519Synechococcus elongatusMutation(s): 2 
Gene Names: kaiCSynpcc7942_1216see0011
EC: 2.7.11.1
UniProt
Find proteins for Q79PF4 (Synechococcus elongatus (strain PCC 7942 / FACHB-805))
Explore Q79PF4 
Go to UniProtKB:  Q79PF4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ79PF4
Protein Feature View
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
ATP (Subject of Investigation/LOI)
Query on ATP

Download Ideal Coordinates CCD File 
BA [auth F],
CA [auth F],
I [auth A],
L [auth B],
M [auth B],
BA [auth F],
CA [auth F],
I [auth A],
L [auth B],
M [auth B],
P [auth C],
Q [auth C],
U [auth D],
X [auth E],
Y [auth E]
ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
 Ligand Interaction
ADP (Subject of Investigation/LOI)
Query on ADP

Download Ideal Coordinates CCD File 
H [auth A],
T [auth D]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
 Ligand Interaction
MG (Subject of Investigation/LOI)
Query on MG

Download Ideal Coordinates CCD File 
AA [auth F],
DA [auth F],
G [auth A],
J [auth A],
K [auth B],
AA [auth F],
DA [auth F],
G [auth A],
J [auth A],
K [auth B],
N [auth B],
O [auth C],
R [auth C],
S [auth D],
V [auth D],
W [auth E],
Z [auth E]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report




Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute on Aging (NIH/NIA)United StatesR21GM142196

Revision History  (Full details and data files)

  • Version 1.0: 2021-09-22
    Type: Initial release