9S6C | pdb_00009s6c

B12 Binding protein - BtuK1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.82 Å
  • R-Value Free: 
    0.192 (Depositor), 0.195 (DCC) 
  • R-Value Work: 
    0.163 (Depositor), 0.164 (DCC) 

Starting Model: in silico
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.0 of the entry. See complete history


Literature

B12 Binding protein - BtuK1

Clarke, C.Banasik, M.Pickersgill, R.W.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Quinoprotein amine dehydrogenase-like proteinA [auth C]337Bacteroides thetaiotaomicronMutation(s): 0 
Gene Names: BT_1486
UniProt
Find proteins for Q8A7N8 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50))
Explore Q8A7N8 
Go to UniProtKB:  Q8A7N8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8A7N8
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Quinoprotein amine dehydrogenase-like proteinB [auth A],
C [auth B]
339Bacteroides thetaiotaomicronMutation(s): 0 
Gene Names: BT_1486
UniProt
Find proteins for Q8A7N8 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50))
Explore Q8A7N8 
Go to UniProtKB:  Q8A7N8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8A7N8
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.82 Å
  • R-Value Free:  0.192 (Depositor), 0.195 (DCC) 
  • R-Value Work:  0.163 (Depositor), 0.164 (DCC) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.739α = 90
b = 129.984β = 90
c = 164.66γ = 90
Software Package:
Software NamePurpose
Aimlessdata scaling
gemmidata extraction
REFMACrefinement
autoPROCdata reduction
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research Council (BBSRC)United Kingdom--

Revision History  (Full details and data files)

  • Version 1.0: 2025-09-17
    Type: Initial release