1DL5

PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.182 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair.

Skinner, M.M.Puvathingal, J.M.Walter, R.L.Friedman, A.M.

(2000) Structure 8: 1189-1201

  • DOI: https://doi.org/10.1016/s0969-2126(00)00522-0
  • Primary Citation of Related Structures:  
    1DL5

  • PubMed Abstract: 

    Formation of isoaspartyl residues is one of several processes that damage proteins as they age. Protein L-isoaspartate (D-aspartate) O-methyltransferase (PIMT) is a conserved and nearly ubiquitous enzyme that catalyzes the repair of proteins damaged by isoaspartyl formation.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University , West Lafayette, IN 47907, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE
A, B
317Thermotoga maritimaMutation(s): 0 
EC: 2.1.1.77
UniProt
Find proteins for Q56308 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q56308 
Go to UniProtKB:  Q56308
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ56308
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SAH
Query on SAH

Download Ideal Coordinates CCD File 
L [auth A],
W [auth B]
S-ADENOSYL-L-HOMOCYSTEINE
C14 H20 N6 O5 S
ZJUKTBDSGOFHSH-WFMPWKQPSA-N
CD
Query on CD

Download Ideal Coordinates CCD File 
C [auth A]
F [auth A]
I [auth A]
J [auth A]
K [auth A]
C [auth A],
F [auth A],
I [auth A],
J [auth A],
K [auth A],
M [auth B],
P [auth B],
S [auth B],
V [auth B]
CADMIUM ION
Cd
WLZRMCYVCSSEQC-UHFFFAOYSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
D [auth A]
E [auth A]
G [auth A]
H [auth A]
N [auth B]
D [auth A],
E [auth A],
G [auth A],
H [auth A],
N [auth B],
O [auth B],
Q [auth B],
R [auth B],
T [auth B],
U [auth B]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.182 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 51.06α = 90
b = 98.91β = 105.66
c = 76.86γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MLPHAREphasing
CNSrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-12-08
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-03-13
    Changes: Data collection, Database references, Derived calculations, Source and taxonomy, Structure summary