3M0W

Structure of S100A4 with PCP


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.302 
  • R-Value Work: 0.252 
  • R-Value Observed: 0.254 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Structure of S100A4 with PCP

Ramagopal, U.A.Dulyaninova, N.G.Almo, S.C.Bresnick, A.R.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein S100-A4
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
100Homo sapiensMutation(s): 0 
Gene Names: CAPLMTS1S100A4
UniProt & NIH Common Fund Data Resources
Find proteins for P26447 (Homo sapiens)
Explore P26447 
Go to UniProtKB:  P26447
PHAROS:  P26447
GTEx:  ENSG00000196154 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26447
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
P77
Query on P77

Download Ideal Coordinates CCD File 
BA [auth F]
EA [auth G]
HA [auth H]
K [auth A]
KA [auth I]
BA [auth F],
EA [auth G],
HA [auth H],
K [auth A],
KA [auth I],
LA [auth I],
O [auth B],
OA [auth J],
R [auth B],
S [auth C],
V [auth D],
Y [auth E]
2-chloro-10-[3-(4-methylpiperazin-1-yl)propyl]-10H-phenothiazine
C20 H24 Cl N3 S
WIKYUJGCLQQFNW-UHFFFAOYSA-N
DIO
Query on DIO

Download Ideal Coordinates CCD File 
N [auth A],
RA [auth J]
1,4-DIETHYLENE DIOXIDE
C4 H8 O2
RYHBNJHYFVUHQT-UHFFFAOYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
AA [auth E]
CA [auth F]
DA [auth F]
FA [auth G]
GA [auth G]
AA [auth E],
CA [auth F],
DA [auth F],
FA [auth G],
GA [auth G],
IA [auth H],
JA [auth H],
L [auth A],
M [auth A],
MA [auth I],
NA [auth I],
P [auth B],
PA [auth J],
Q [auth B],
QA [auth J],
T [auth C],
U [auth C],
W [auth D],
X [auth D],
Z [auth E]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.302 
  • R-Value Work: 0.252 
  • R-Value Observed: 0.254 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.577α = 90
b = 102.275β = 92.6
c = 117.37γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
CBASSdata collection
HKL-2000data reduction
MOLREPphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-05-12
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2017-11-08
    Changes: Refinement description
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description