1YPN

REDUCED FORM HYDROXYMETHYLBILANE SYNTHASE (K59Q MUTANT) CRYSTAL STRUCTURE AFTER 2 HOURS IN A FLOW CELL DETERMINED BY TIME-RESOLVED LAUE DIFFRACTION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.199 

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Ligand Structure Quality Assessment 


This is version 1.5 of the entry. See complete history. 


Literature

Time-Resolved Structures of Hydroxymethylbilane Synthase (Lys59Gln Mutant) as It Isloaded with Substrate in the Crystal Determined by Laue Diffraction

Helliwell, J.R., Nieh, Y.P., Cassetta, A., Habash, J., Carr, P.D., Ursby, T., Wulff, M., Thompson, A.W., Niemann, A.C., Haedener, A.

(1998) J Chem Soc Faraday Trans 94: 2615-2622


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HYDROXYMETHYLBILANE SYNTHASE313Escherichia coliMutation(s): 1 
EC: 2.5.1.61
UniProt
Find proteins for P06983 (Escherichia coli (strain K12))
Explore P06983 
Go to UniProtKB:  P06983
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06983
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DPM
Query on DPM
Download Ideal Coordinates CCD File 
B [auth A]3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid
C20 H24 N2 O8
LCAXMKQKEYTFDM-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.199 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 88.47α = 90
b = 76.15β = 90
c = 50.79γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DARESBURYdata reduction
LAUENORMdata scaling
CCP4data scaling
X-PLORphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-03-02
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2013-09-18
    Changes: Non-polymer description
  • Version 1.4: 2021-11-03
    Changes: Database references, Derived calculations, Other
  • Version 1.5: 2023-08-09
    Changes: Refinement description