3IWE

Crystal Structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD85646


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.79 Å
  • R-Value Free: 
    0.219 (Depositor), 0.220 (DCC) 
  • R-Value Work: 
    0.180 (Depositor), 0.180 (DCC) 
  • R-Value Observed: 
    0.182 (Depositor) 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted MYAClick on this verticalbar to view detailsBest fitted 646Click on this verticalbar to view details

This is version 1.4 of the entry. See complete history


Literature

Crystal Structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD85646

Qiu, W.Hutchinson, A.Wernimont, A.Lin, Y.-H.Kania, A.Ravichandran, M.Kozieradzki, I.Cossar, D.Schapira, M.Arrowsmith, C.H.Bountra, C.Weigelt, J.Edwards, A.M.Wyatt, P.G.Ferguson, M.A.J.Frearson, J.A.Brand, S.Y.Robinson, D.A.Bochkarev, A.Hui, R.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glycylpeptide N-tetradecanoyltransferase 1
A, B
383Homo sapiensMutation(s): 0 
Gene Names: NMTNMT1
EC: 2.3.1.97 (PDB Primary Data), 2.3.1 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P30419 (Homo sapiens)
Explore P30419 
Go to UniProtKB:  P30419
PHAROS:  P30419
GTEx:  ENSG00000136448 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP30419
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
646 BindingDB:  3IWE Ki: min: 4, max: 300 (nM) from 13 assay(s)
IC50: min: 3, max: 4 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.79 Å
  • R-Value Free:  0.219 (Depositor), 0.220 (DCC) 
  • R-Value Work:  0.180 (Depositor), 0.180 (DCC) 
  • R-Value Observed: 0.182 (Depositor) 
Space Group: P 2 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.287α = 90
b = 77.654β = 90
c = 179.568γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
PHASERphasing
REFMACrefinement
XDSdata reduction
XDSdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted MYAClick on this verticalbar to view detailsBest fitted 646Click on this verticalbar to view details

Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2009-09-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2011-10-12
    Changes: Atomic model
  • Version 1.3: 2011-11-16
    Changes: Other
  • Version 1.4: 2024-02-21
    Changes: Data collection, Database references, Derived calculations