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Article title matches
- Category:Thif (35 bytes)
1: List of pages with the keyword Thif - Category:Uba/thif-type nad/fad binding fold (65 bytes)
1: List of pages with the keyword Uba/thif-type nad/fad binding fold
Page text matches
- 1zfn (2,567 bytes)
2: ==Structural Analysis of Escherichia coli ThiF==
11: [https://www.uniprot.org/uniprot/THIF_ECOLI THIF_ECOLI] Catalyzes the adenylation by ATP of the ca... - 1zkm (2,501 bytes)
2: ==Structural Analysis of Escherichia Coli ThiF==
11: [https://www.uniprot.org/uniprot/THIF_ECOLI THIF_ECOLI] Catalyzes the adenylation by ATP of the ca... - 1zud (4,001 bytes)
2: ==Structure of ThiS-ThiF protein complex==
11: [https://www.uniprot.org/uniprot/THIF_ECOLI THIF_ECOLI] Catalyzes the adenylation by ATP of the ca...
24: ... the molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies the mechanism of the sul...
26: Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer s... - Category:Thif (35 bytes)
1: List of pages with the keyword Thif - 3dwg (4,988 bytes)
24: ...ments that contribute to complex formation in the ThiF-ThiS and MoeB-MoaD systems, despite major differe... - 3dwi (4,992 bytes)
24: ...ments that contribute to complex formation in the ThiF-ThiS and MoeB-MoaD systems, despite major differe... - 3dwm (4,484 bytes)
23: ...ments that contribute to complex formation in the ThiF-ThiS and MoeB-MoaD systems, despite major differe... - Category:Uba/thif-type nad/fad binding fold (65 bytes)
1: List of pages with the keyword Uba/thif-type nad/fad binding fold - 4rdh (4,110 bytes)
14: ... an active cysteine, similar to the mechanisms in ThiF and MoeB, could take place for the dehydratase fu... - 4rdi (4,059 bytes)
14: ... an active cysteine, similar to the mechanisms in ThiF and MoeB, could take place for the dehydratase fu... - 4yed (3,982 bytes)
14: ... an active cysteine, similar to the mechanisms in ThiF and MoeB, could take place for the dehydratase fu... - 8t19 (1,667 bytes)
2: ... peptide recognition element (RRE) domain of Ocin-ThiF-like partner protein, PbtF, bound to an 8 residue...
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