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5IJA

[NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis

Summary for 5IJA
Entry DOI10.2210/pdb5ija/pdb
DescriptorHydrogenase-specific maturation endopeptidase (2 entities in total)
Functional Keywordshydrogenase maturation protease, hydrolase
Biological sourceThermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Total number of polymer chains2
Total formula weight32668.23
Authors
Kwon, S.,Nishitani, Y.,Watanabe, S.,Miki, K. (deposition date: 2016-03-01, release date: 2016-06-01, Last modification date: 2023-11-08)
Primary citationKwon, S.,Nishitani, Y.,Watanabe, S.,Hirao, Y.,Imanaka, T.,Kanai, T.,Atomi, H.,Miki, K.
Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1
Proteins, 84:1321-1327, 2016
Cited by
PubMed Abstract: A [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1 (TkHybD) is involved in the cleavage of the C-terminal residues of [NiFe] hydrogenase large subunits by Ni recognition. Here, we report the crystal structure of TkHybD at 1.82 Å resolution to better understand this process. TkHybD exhibits an α/β/α sandwich fold with conserved residues responsible for the Ni recognition. Comparisons of TkHybD with homologous proteins also reveal that they share a common overall architecture, suggesting that they have similar catalytic functions. Our results including metal binding site prediction provide insight into the substrate recognition and catalysis mechanism of TkHybD. Proteins 2016; 84:1321-1327. © 2016 Wiley Periodicals, Inc.
PubMed: 27192667
DOI: 10.1002/prot.25070
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.82 Å)
Structure validation

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