The X-ray crystal structure of the 65kDa isoform of Glutamic Acid Decarboxylase (GAD65). Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Mar 2007.
Explore 2OKK in 3D Show helices and sheets RCSB PDB PDBe
2OKK contains 27 α-helices and 17 β-strands across 1 chain. 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 | 89-91 | 3 | |
| α-helix | 94-96 | 3 | |
| α-helix | 104-126 | 23 | |
| α-helix | 138-144 | 7 | |
| α-helix | 153-155 | 3 | |
| α-helix | 156-169 | 14 | |
| β-strand | 178-179 | 2 | 1 |
| α-helix | 188-200 | 13 | |
| α-helix | 211-228 | 18 | |
| α-helix | 231-233 | 3 | |
| β-strand | 236-240 | 5 | 2 |
| α-helix | 243-258 | 16 | |
| α-helix | 262-265 | 4 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-278 | 6 | 2 |
| α-helix | 284-291 | 8 | |
| α-helix | 296-298 | 3 | |
| β-strand | 299-302 | 4 | 2 |
| α-helix | 303 | 1 | |
| β-strand | 304 | 1 | 3 |
| β-strand | 310 | 1 | 3 |
| α-helix | 312-324 | 13 | |
| β-strand | 328-335 | 8 | 2 |
| β-strand | 336 | 1 | 4 |
| β-strand | 344 | 1 | 4 |
| α-helix | 347-357 | 11 | |
| β-strand | 360-365 | 6 | 2 |
| α-helix | 368-373 | 6 | |
| α-helix | 378-381 | 4 | |
| α-helix | 384-386 | 3 | |
| β-strand | 389-392 | 4 | 2 |
| β-strand | 405-409 | 5 | 2 |
| α-helix | 414-419 | 6 | |
| α-helix | 435-437 | 3 | |
| α-helix | 440-442 | 3 | |
| α-helix | 452-486 | 35 | |
| β-strand | 491-493 | 3 | 5 |
| β-strand | 504-508 | 5 | 5 |
| α-helix | 523-526 | 4 | |
| α-helix | 529-540 | 12 | |
| β-strand | 544-545 | 2 | 1 |
| β-strand | 546-550 | 5 | 5 |
| β-strand | 553-559 | 7 | 5 |
| α-helix | 568-581 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate decarboxylase 2 | A | protein | 497 | Homo sapiens | Q05329 (AlphaFold model) |
>2OKK_1 Glutamate decarboxylase 2 (chains A) NYAFLHATDLLPACDGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNW ELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTY EIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMMIARFKMFPEVKEKGM AALPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEAKQKGF VPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERA NSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQMHASYLFQQDKHYDLSYDTGDKALQCG RHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFW YIPPSLRTLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAAT HQDIDFLIEEIERLGQD
| ID | Name | Formula | Copies |
|---|---|---|---|
| ABU | Gamma-amino-butanoic acid | C4 H9 N O2 | 2 |
Water and common crystallization additives (GOL) are not listed.
GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Fenalti, G., Law, R.H., Buckle, A.M. et al. Nat Struct Mol Biol (2007) 14:280-286. DOI 10.1038/nsmb1228 · PubMed
Other PDB entries of the same protein (UniProt Q05329 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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