1SXS | pdb_00001sxs

Reduced bovine superoxide dismutase at pH 5.0 complexed with thiocyanate

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 
    0.175 (Depositor) 

Starting Model: experimental
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This is version 1.4 of the entry. See complete history. 


Literature

Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site

Ferraroni, M., Rypniewski, W.R., Bruni, B., Orioli, P., Mangani, S.

(1998) J Biol Inorg Chem 3: 411-422


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (CU-ZN SUPEROXIDE DISMUTASE)
A, B
151Bos taurusMutation(s): 0 
EC: 1.15.1.1
UniProt
Find proteins for P00442 (Bos taurus)
Explore P00442 
Go to UniProtKB:  P00442
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00442
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN
Download Ideal Coordinates CCD File 
E [auth A],
I [auth B]		ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
CU
Query on CU
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D [auth A],
H [auth B]		COPPER (II) ION
Cu
JPVYNHNXODAKFH-UHFFFAOYSA-N
SCN
Query on SCN
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C [auth A],
G [auth B]		THIOCYANATE ION
C N S
ZMZDMBWJUHKJPS-UHFFFAOYSA-M
CA
Query on CA
Download Ideal Coordinates CCD File 
F [auth A],
J [auth B]		CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work:  0.175 (Depositor) 
Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 104.6α = 90
b = 197.5β = 90
c = 50.8γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CCP4refinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-09-30
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-23
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.4: 2024-11-20
    Changes: Structure summary