Human CDC7 kinase in complex with DBF4 and nucleotide. Determined by X-ray diffraction at 2.17 Å resolution. Released 31 Oct 2012.
Explore 4F9A in 3D Show helices and sheets RCSB PDB PDBe
4F9A contains 49 α-helices and 36 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-50 | 11 | |
| α-helix | 52-56 | 5 | |
| β-strand | 59-66 | 8 | 1 |
| β-strand | 70-78 | 9 | 1 |
| β-strand | 79 | 1 | 2 |
| β-strand | 84-92 | 9 | 1 |
| α-helix | 93 | 1 | |
| α-helix | 98-110 | 13 | |
| β-strand | 114 | 1 | 3 |
| β-strand | 117 | 1 | 3 |
| β-strand | 122-126 | 5 | 1 |
| β-strand | 129-135 | 7 | 1 |
| α-helix | 142-146 | 5 | |
| α-helix | 151-170 | 20 | |
| β-strand | 173-174 | 2 | 4 |
| α-helix | 180-182 | 3 | |
| β-strand | 183-186 | 4 | 3 |
| β-strand | 191-194 | 4 | 3 |
| β-strand | 201-202 | 2 | 4 |
| α-helix | 209-213 | 5 | |
| α-helix | 377-379 | 3 | |
| α-helix | 382-385 | 4 | |
| α-helix | 394-409 | 16 | |
| α-helix | 420-431 | 12 | |
| α-helix | 433-441 | 9 | |
| β-strand | 445-449 | 5 | 5 |
| α-helix | 454-457 | 4 | |
| α-helix | 458-465 | 8 | |
| α-helix | 540-549 | 10 | |
| α-helix | 560-564 | 5 | |
| α-helix | 567-569 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 215-216 | 2 | |
| β-strand | 219-224 | 6 | 5 |
| β-strand | 232-235 | 4 | 5 |
| α-helix | 247 | 1 | |
| β-strand | 295-296 | 2 | 6 |
| β-strand | 301-302 | 2 | 6 |
| α-helix | 306-309 | 4 | |
| α-helix | 313-320 | 8 | |
| α-helix | 325-331 | 7 | |
| α-helix | 335-336 | 2 | |
| β-strand | 338 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 38-50 | 13 | |
| α-helix | 52-56 | 5 | |
| β-strand | 59-66 | 8 | 7 |
| β-strand | 70-78 | 9 | 7 |
| β-strand | 79 | 1 | 8 |
| β-strand | 84-92 | 9 | 7 |
| α-helix | 93 | 1 | |
| α-helix | 98-110 | 13 | |
| β-strand | 114 | 1 | 9 |
| β-strand | 117 | 1 | 9 |
| β-strand | 122-126 | 5 | 7 |
| β-strand | 129-135 | 7 | 7 |
| α-helix | 142-146 | 5 | |
| α-helix | 151-170 | 20 | |
| β-strand | 173-174 | 2 | 10 |
| α-helix | 180-182 | 3 | |
| β-strand | 183-186 | 4 | 9 |
| β-strand | 191-194 | 4 | 9 |
| β-strand | 201-202 | 2 | 10 |
| α-helix | 209-212 | 4 | |
| α-helix | 377-379 | 3 | |
| α-helix | 382-385 | 4 | |
| α-helix | 394-409 | 16 | |
| α-helix | 420-431 | 12 | |
| α-helix | 433-442 | 10 | |
| β-strand | 445-449 | 5 | 11 |
| α-helix | 454-457 | 4 | |
| α-helix | 458-465 | 8 | |
| α-helix | 540-549 | 10 | |
| α-helix | 558-559 | 2 | |
| α-helix | 560-564 | 5 | |
| α-helix | 567-569 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 215-216 | 2 | |
| β-strand | 219-224 | 6 | 11 |
| β-strand | 232-235 | 4 | 11 |
| β-strand | 295-296 | 2 | 12 |
| β-strand | 301-302 | 2 | 12 |
| α-helix | 306-311 | 6 | |
| α-helix | 313-319 | 7 | |
| α-helix | 322-324 | 3 | |
| α-helix | 325-331 | 7 | |
| α-helix | 335-336 | 2 | |
| β-strand | 338 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division cycle 7-related protein kinase | A, C | protein | 361 | Homo sapiens | O00311 (AlphaFold model) |
| Protein DBF4 homolog A | B, D | protein | 144 | Homo sapiens | Q9UBU7 (AlphaFold model) |
>4F9A_1 Cell division cycle 7-related protein kinase (chains A, C) MLAGVKKDIEKLYEAVPQLSNVFKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPT SHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVR EYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQ SEAQQERCSQNKCSICLSRRQQVAPRAGTPGFRAPEVLTKCPNQTTAIDMWSAGVIFLSL LSGRYPFYKASDDLTALAQIMTIRGSRETIQAAKTFGKSILCSKEVPAQDLRKLCERLRG MDSSTPKLTSDIQGHATNLEGWNEVPDEAYDLLDKLLDLNPASRITAEEALLHPFFKDMS L
>4F9A_2 Protein DBF4 homolog A (chains B, D) GPGTRTGRLKKPFVKVEDMSQLYRPFYLQLTNMPFINYSIQKPCSPFDVDKPSSMQKQTQ VKLRIQTDGDKYGGTSIQLQLKEKKKKGYCECCLQKYEDLETHLLSEQHRNFAQSNQYQV VDDIVSKLVFDFVEYEKDTPKKKR
Crystal structure of human CDC7 kinase in complex with its activator DBF4. Hughes, S., Elustondo, F., Di Fonzo, A. et al. Nat Struct Mol Biol (2012) 19:1101-1107. DOI 10.1038/nsmb.2404 · PubMed
Other PDB entries of the same protein (UniProt O00311 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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