Crystal structure of human gamma-tubulin bound to GDP. Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Jun 2008.
Explore 3CB2 in 3D Show helices and sheets RCSB PDB PDBe
3CB2 contains 52 α-helices and 36 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 5-10 | 6 | 1 |
| α-helix | 11-28 | 18 | |
| β-strand | 31 | 1 | 2 |
| α-helix | 36 | 1 | |
| β-strand | 37 | 1 | 2 |
| α-helix | 38 | 1 | |
| α-helix | 41-42 | 2 | |
| α-helix | 48-50 | 3 | |
| β-strand | 52-54 | 3 | 3 |
| β-strand | 60-62 | 3 | 3 |
| β-strand | 64-68 | 5 | 1 |
| α-helix | 72-79 | 8 | |
| α-helix | 88-90 | 3 | |
| β-strand | 91-93 | 3 | 1 |
| α-helix | 104-127 | 24 | |
| β-strand | 134-140 | 7 | 1 |
| α-helix | 145-149 | 5 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165-172 | 8 | 1 |
| α-helix | 173 | 1 | |
| α-helix | 184-197 | 14 | |
| β-strand | 201-206 | 6 | 1 |
| α-helix | 207-216 | 10 | |
| α-helix | 225-239 | 15 | |
| α-helix | 253-260 | 8 | |
| β-strand | 268-269 | 2 | 1 |
| β-strand | 270-274 | 5 | 4 |
| α-helix | 287-289 | 3 | |
| α-helix | 290-296 | 7 | |
| α-helix | 300-302 | 3 | |
| β-strand | 303 | 1 | 4 |
| β-strand | 317-325 | 9 | 4 |
| α-helix | 330-342 | 13 | |
| β-strand | 348 | 1 | 4 |
| β-strand | 356-361 | 6 | 4 |
| α-helix | 362-364 | 3 | |
| β-strand | 374-381 | 8 | 4 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-400 | 16 | |
| α-helix | 406-409 | 4 | |
| α-helix | 412-414 | 3 | |
| α-helix | 419-437 | 19 | |
| α-helix | 441-443 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-10 | 7 | 5 |
| α-helix | 11-28 | 18 | |
| β-strand | 31 | 1 | 6 |
| β-strand | 36 | 1 | 7 |
| β-strand | 37 | 1 | 6 |
| α-helix | 38 | 1 | |
| α-helix | 39-41 | 3 | |
| β-strand | 52-54 | 3 | 8 |
| β-strand | 59 | 1 | 7 |
| β-strand | 60-62 | 3 | 8 |
| β-strand | 64-68 | 5 | 5 |
| α-helix | 72-78 | 7 | |
| α-helix | 88-90 | 3 | |
| β-strand | 91-93 | 3 | 5 |
| α-helix | 104-113 | 10 | |
| α-helix | 115-127 | 13 | |
| β-strand | 132-140 | 9 | 5 |
| α-helix | 145-160 | 16 | |
| β-strand | 165-172 | 8 | 5 |
| α-helix | 173-174 | 2 | |
| α-helix | 175-180 | 6 | |
| α-helix | 184-197 | 14 | |
| β-strand | 201-206 | 6 | 5 |
| α-helix | 207-216 | 10 | |
| α-helix | 225-239 | 15 | |
| α-helix | 241-244 | 4 | |
| α-helix | 249-251 | 3 | |
| α-helix | 253-260 | 8 | |
| β-strand | 268-269 | 2 | 5 |
| β-strand | 270-274 | 5 | 9 |
| α-helix | 290-298 | 9 | |
| α-helix | 300-302 | 3 | |
| β-strand | 303 | 1 | 9 |
| β-strand | 317-325 | 9 | 9 |
| α-helix | 330-332 | 3 | |
| α-helix | 333-342 | 10 | |
| β-strand | 348 | 1 | 9 |
| β-strand | 356-361 | 6 | 9 |
| β-strand | 374-381 | 8 | 9 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 406-409 | 4 | |
| α-helix | 412-414 | 3 | |
| α-helix | 419-437 | 19 | |
| α-helix | 441-443 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| tubulin gamma-1 chain | A, B | protein | 475 | Homo sapiens | P23258 (AlphaFold model) |
>3CB2_1 tubulin gamma-1 chain (chains A, B) MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEAIVEEFATEGTDRKDVFFYQADDEHY IPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFD IIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSD VVVQPYNSLLTLKRLTQNADCLVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSAST TTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQP KNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVAL SRKSPYLPSAHRVSGLMMANHTSISSLFERTCRQYDKLRKREAFLEQFRKEDMFKDNFDE MDTSREIVQQLIDEYHAATRPDYISWGTQEQVDVDGGQKLISEEDLLLEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
The lattice as allosteric effector: structural studies of alphabeta- and gamma-tubulin clarify the role of GTP in microtubule assembly. Rice, L.M., Montabana, E.A., Agard, D.A. Proc Natl Acad Sci U S A (2008) 105:5378-5383. DOI 10.1073/pnas.0801155105 · PubMed
Other PDB entries of the same protein (UniProt P23258 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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