Summary for 1P4M
| Entry DOI | 10.2210/pdb1p4m/pdb |
| Related | 1NB0 1NB9 |
| Descriptor | RIBOFLAVIN KINASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | beta barrel, riboflavin kinase, flavin mononucleotide, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm (By similarity): Q969G6 |
| Total number of polymer chains | 1 |
| Total formula weight | 17679.93 |
| Authors | Karthikeyan, S.,Zhou, Q.,Mseeh, F.,Grishin, N.V.,Osterman, A.L.,Zhang, H. (deposition date: 2003-04-23, release date: 2003-05-13, 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 Cited by 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: 12623014DOI: 10.1016/S0969-2126(03)00024-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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