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6JBP

Structure of MP-4 from Mucuna pruriens at 2.22 Angstroms

Summary for 6JBP
Entry DOI10.2210/pdb6jbp/pdb
Related5DSS
DescriptorKunitz-type trypsin inhibitor-like 2 protein (2 entities in total)
Functional Keywordsprotease inhibitor, mucuna pruriens, plant protein
Biological sourceMucuna pruriens (Velvet bean)
Total number of polymer chains1
Total formula weight20110.43
Authors
Jain, A.,Shikhi, M.,Kumar, A.,Kumar, A.,Nair, D.T.,Salunke, D.M. (deposition date: 2019-01-26, release date: 2020-01-29, Last modification date: 2024-11-20)
Primary citationJain, A.,Kumar, A.,Shikhi, M.,Kumar, A.,Nair, D.T.,Salunke, D.M.
The structure of MP-4 from Mucuna pruriens at 2.22 angstrom resolution.
Acta Crystallogr.,Sect.F, 76:47-57, 2020
Cited by
PubMed 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.
PubMed: 32039885
DOI: 10.1107/S2053230X20000199
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.217 Å)
Structure validation

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