International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F. ch. 23.2, p. 587   | 1 | 2 |

Figure 23.2.5.3 

A. E. Hodela and F. A. Quiochob

aDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA, and  bHoward Hughes Medical Institute and Department of Biochemistry, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA

[Figure 23.2.5.3]
Figure 23.2.5.3

Electrostatic surface potential of (a) the phosphate-binding protein and (b) flavodoxin. The molecular surface electrostatic potentials, calculated and displayed using GRASP (Nicholls et al., 1991[link]), are −10 kT (red), neutral (white) and +10 kT (blue) [see Ledvina et al. (1996)[link] for more details]. (a) Wild-type phosphate-binding protein based on the X-ray structure of the open cleft, unliganded form (Ledvina et al., 1996[link]). The phosphate-binding site is located in the cleft (with negative surface potential) in the middle of the molecule and between the two domains. (b) Flavodoxin with bound flavin mononucleotide (FMN). The phosphoryl group (P) of the FMN is bound in a pocket with intense negatively charge surface potential. The surface potential was calculated without the bound flavin mononucleotide using the structure from the Protein Data Bank (PDB code: 2fox).