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4GHK

X-ray Crystal Structure of Gamma-glutamyl phosphate reductase from Burkholderia thailandensis

Summary for 4GHK
Entry DOI10.2210/pdb4ghk/pdb
DescriptorGamma-glutamyl phosphate reductase (2 entities in total)
Functional Keywordsstructural genomics, niaid, national institute of allergy and infectious diseases, seattle structural genomics center for infectious disease, ssgcid, gamma-glutamyl phosphate reductase, oxidoreductase
Biological sourceBurkholderia thailandensis
Cellular locationCytoplasm (By similarity): Q2SZ88
Total number of polymer chains4
Total formula weight190636.72
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-08-07, release date: 2012-12-26, Last modification date: 2023-09-13)
Primary citationBaugh, L.,Gallagher, L.A.,Patrapuvich, R.,Clifton, M.C.,Gardberg, A.S.,Edwards, T.E.,Armour, B.,Begley, D.W.,Dieterich, S.H.,Dranow, D.M.,Abendroth, J.,Fairman, J.W.,Fox, D.,Staker, B.L.,Phan, I.,Gillespie, A.,Choi, R.,Nakazawa-Hewitt, S.,Nguyen, M.T.,Napuli, A.,Barrett, L.,Buchko, G.W.,Stacy, R.,Myler, P.J.,Stewart, L.J.,Manoil, C.,Van Voorhis, W.C.
Combining functional and structural genomics to sample the essential Burkholderia structome.
Plos One, 8:e53851-e53851, 2013
Cited by
PubMed Abstract: The genus Burkholderia includes pathogenic gram-negative bacteria that cause melioidosis, glanders, and pulmonary infections of patients with cancer and cystic fibrosis. Drug resistance has made development of new antimicrobials critical. Many approaches to discovering new antimicrobials, such as structure-based drug design and whole cell phenotypic screens followed by lead refinement, require high-resolution structures of proteins essential to the parasite.
PubMed: 23382856
DOI: 10.1371/journal.pone.0053851
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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