1p4m | pdb_00001p4m
CRYSTAL STRUCTURE OF RIBOFLAVIN KINASE
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| 1p4m, resolution 1.80Å | |||||||||||||
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| Ligands: | MG, ADP and FMN | ||||||||||||
| Gene: | FLJ11149 (Homo sapiens) | ||||||||||||
| Activity: | Riboflavin kinase, with EC number 2.7.1.26 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1P4M is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1NBG. Full crystallographic information is available from OCA.
Reference
Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch., Karthikeyan S, Zhou Q, Mseeh F, Grishin NV, Osterman AL, Zhang H, Structure. 2003 Mar;11(3):265-73. PMID:12623014
Page seeded by OCA on Thu Mar 20 13:19:46 2008
