Table 1. Surface residues with low B factors, which are potentially important for binding.
| Residue | B factor | Exposed surface, % | Amino acid replacements in the homologous sequences† | Interface binding site | No. of known cancer mutations |
|---|---|---|---|---|---|
| His-178 | 25.2 | 59.9 | H (10) | A—B* | 12 (frameshift) |
| Glu-171 | 25.3 | 37.7 | D (3) E (7) | A*—B | |
| His-233 | 25.9 | 36.9 | H (5) L (5) | B—C* | 3 (His233Asp) |
| Tyr-107 | 26.5 | 25.7 | H (1) L (1) Y (8) | ||
| His-168 | 26.6 | 25.9 | D (1) H (7) F (1) Y (1) | DNA binding from A | |
| Asn-210 | 26.7 | 67.1 | N (5) Q (2) H (1) I (1) Y (1) | A*—B, B*—C | 10 (frameshift + Asn210Tyr) |
| Arg-174 | 27.6 | 46.1 | R (9) K (1) | A*—B | 6 (Arg174Ala) |
| Asn-131 | 28.1 | 37.1 | N (9) K (1) | ||
| Lys-101 | 28.5 | 78.9 | D (1) K (5) S (2) T (2) | B*—C (DNA—b—A) | |
| Ala-138 | 28.6 | 33.7 | A (10) | A—B* | 12 (Ala138Ser; Ala138Pro) |
| Leu-137 | 28.9 | 25.8 | L (10) | A—B* | |
| Trp-146 | 34.6 | 34.6 | R (2) L (1) W (5) V (2) | ||
| Phe-212 | 38.0 | 65.9 | G (1) L (2) K (2) F (5) | A*—B | 5 (frameshift) |
| Met-243 | 38.7 | 69.9 | M (10) |
Bold indicates absolute conservation.
*
Residue location on interface.
†
Amino acid replacements in the equivalent positions, obtained from the alignment of p53 sequences from the following sources: 1, Homo sapiens (human); 2, Platichthys flesus (European flounder); 3, Oryzias latipes (Medaka fish) (Japanese ricefish); 4, Xenopus laevis (African clawed frog); 5, Oncorhynchus mykiss (rainbow trout) (Salmo gairdneri); 6, Brachydanio rerio (zebrafish) (Danio rerio); 7, Mus musculus (mouse); 8, Cricetulus griseus (Chinese hamster); 9, Bos taurus (bovine); 10, Felis silvestris catus (cat).