5C6H

Mcl-1 complexed with Mule


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.346 
  • R-Value Work: 0.295 
  • R-Value Observed: 0.297 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of Mcl-1 complexed with Mule at 2.05 Angstroms resolution

Song, T.Wang, Z.Ji, F.Chai, G.Liu, Y.Li, X.Li, Z.Fan, Y.Zhang, Z.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Induced myeloid leukemia cell differentiation protein Mcl-1
A, C, E, G, I
A, C, E, G, I, K, M, O, Q, S, U, W
157Homo sapiensMutation(s): 0 
Gene Names: MCL1BCL2L3
UniProt & NIH Common Fund Data Resources
Find proteins for Q07820 (Homo sapiens)
Explore Q07820 
Go to UniProtKB:  Q07820
PHAROS:  Q07820
GTEx:  ENSG00000143384 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ07820
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Mule BH3 peptide from E3 ubiquitin-protein ligase HUWE1
B, D, F, H, J
B, D, F, H, J, L, N, P, R, T, V, X
26Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q7Z6Z7 (Homo sapiens)
Explore Q7Z6Z7 
Go to UniProtKB:  Q7Z6Z7
PHAROS:  Q7Z6Z7
GTEx:  ENSG00000086758 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7Z6Z7
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.346 
  • R-Value Work: 0.295 
  • R-Value Observed: 0.297 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 31.79α = 90.12
b = 114.24β = 92.32
c = 135.98γ = 90.01
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data collection
PHENIXmodel building
Cootdata processing
XDSdata reduction
Cootphasing
HKL-2000data extraction

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of ChinaChina21402022
National Natural Science Foundation of ChinaChina21372036

Revision History  (Full details and data files)

  • Version 1.0: 2016-08-03
    Type: Initial release
  • Version 1.1: 2017-10-18
    Changes: Author supporting evidence, Derived calculations
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references