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PDBsum entry 6jbp

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protein links
Plant protein PDB id
6jbp

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
179 a.a.
Waters ×88
PDB id:
6jbp
Name: Plant protein
Title: Structure of mp-4 from mucuna pruriens at 2.22 angstroms
Structure: Kunitz-type trypsin inhibitor-like 2 protein. Chain: b
Source: Mucuna pruriens. Velvet bean. Organism_taxid: 157652
Resolution:
2.22Å     R-factor:   0.181     R-free:   0.220
Authors: A.Jain,M.Shikhi,A.Kumar,A.Kumar,D.T.Nair,D.M.Salunke
Key ref: A.Jain et al. (2020). The structure of MP-4 from Mucuna pruriens at 2.22 Å resolution. Acta Crystallogr F Struct Biol Commun, 76, 47-57. PubMed id: 32039885 DOI: 10.1107/S2053230X20000199
Date:
26-Jan-19     Release date:   29-Jan-20    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
A0A371E4L6  (A0A371E4L6_MUCPR) -  Kunitz-type trypsin inhibitor-like 2 protein (Fragment) from Mucuna pruriens
Seq:
Struc:
216 a.a.
179 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1107/S2053230X20000199 Acta Crystallogr F Struct Biol Commun 76:47-57 (2020)
PubMed id: 32039885  
 
 
The structure of MP-4 from Mucuna pruriens at 2.22 Å resolution.
A.Jain, A.Kumar, M.Shikhi, A.Kumar, D.T.Nair, D.M.Salunke.
 
  ABSTRACT  
 
The structure of the MP-4 protein was previously determined at a resolution of 2.8 Å. Owing to the unavailability of gene-sequence information at the time, the side-chain assignment was carried out on the basis of a partial sequence available through Edman degradation, sequence homology to orthologs and electron density. The structure of MP-4 has now been determined at a higher resolution (2.22 Å) in another space group and all of the structural inferences that were presented in the previous report of the structure were validated. In addition, the present data allowed an improved assignment of side chains and enabled further analysis of the MP-4 structure, and the accuracy of the assignment was confirmed by the recently available gene sequence. The study reinforces the traditional concept that conservative interpretations of relatively low-resolution structures remain correct even with the availability of high-resolution data.
 

 

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