1NB9

Crystal Structure of Riboflavin Kinase

Summary for 1NB9

• Entry DOI: 10.2210/pdb1nb9/pdb
• Related: 1NB0 1nbg
• Descriptor: hypothetical protein FLJ11149, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: transferase, beta barrel, riboflavin, riboflavin kinase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q969G6
• Total number of polymer chains: 1
• Total formula weight: 17599.95

Authors

Karthikeyan, S.,Zhou, Q.,Mseeh, F.,Grishin, N.V.,Osterman, A.L.,Zhang, H. (deposition date: 2002-12-02, release date: 2003-03-11, Last modification date: 2023-08-16)

Primary citation

Karthikeyan, S.,Zhou, Q.,Mseeh, F.,Grishin, N.V.,Osterman, A.L.,Zhang, H.
Crystal Structure of Human Riboflavin Kinase Reveals a Beta Barrel Fold and a Novel Active Site Arch
Structure, 11:265-273, 2003

PubMed Abstract: Riboflavin kinase (RFK) is an essential enzyme catalyzing the phosphorylation of riboflavin (vitamin B(2)) to form FMN, an obligatory step in vitamin B(2) utilization and flavin cofactor synthesis. The structure of human RFK revealed a six-stranded antiparallel beta barrel core structurally similar to the riboflavin synthase/ferredoxin reductase FAD binding domain fold. The binding site of an intrinsically bound MgADP defines a novel nucleotide binding motif that encompasses a loop, a 3(10) helix, and a reverse turn followed by a short beta strand. This active site loop forms an arch with ATP and riboflavin binding at the opposite side and the phosphoryl transfer appears to occur through the hole underneath the arch. The invariant residues Asn36 and Glu86 are implicated in the catalysis.

PubMed: 12623014
DOI: 10.1016/S0969-2126(03)00024-8

Experimental method

X-RAY DIFFRACTION (1.7 Å)