2ZRT: Zn2+-bound form of des3-23ALG-2

Crystal structure of Zn2+-bound form of des3-23ALG-2. Determined by X-ray diffraction at 3.3 Å resolution. Released 4 Nov 2008.

Method
X-ray diffraction
Resolution
3.3 Å
Organism
Homo sapiens
Chains
8
Atoms
11,004
Mol. weight
160.87 kDa
Ligands
ZN
Released
4 Nov 2008

Explore 2ZRT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ZRT contains 64 α-helices and 38 β-strands across 8 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.

Chain A: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix62-698
α-helix87-10317
α-helix113-1219
α-helix148-16821
β-strand175-17621
β-strand17912
α-helix180-1878
Chain B: 8 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix25-3511
β-strand4313
α-helix47-515
α-helix62-698
β-strand8013
α-helix82-10221
β-strand11014
α-helix112-1209
α-helix128-13811
β-strand14614
α-helix148-16821
β-strand17512
β-strand178-17921
α-helix184-1863
Chain C: 8 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix26-349
β-strand43-4425
α-helix45-495
β-strand5316
β-strand5916
α-helix62-7211
β-strand79-8025
α-helix82-10221
β-strand11017
α-helix112-1209
α-helix128-13811
β-strand14617
α-helix148-16821
β-strand175-17958
α-helix180-1878
Chain D: 9 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix28-358
β-strand4319
α-helix45-506
α-helix59-602
α-helix62-7211
β-strand8019
α-helix82-10120
β-strand110110
α-helix112-12211
α-helix128-13811
β-strand146110
α-helix148-16619
β-strand175-17958
α-helix180-1878
Chain E: 8 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix25-3511
β-strand43111
α-helix47-504
α-helix62-7211
β-strand80111
α-helix82-10019
β-strand110112
α-helix112-1198
α-helix130-1378
β-strand146112
α-helix148-16821
β-strand176-178313
α-helix180-1878
Chain F: 9 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix26-3510
β-strand43-44214
α-helix45-495
α-helix59-613
α-helix62-7211
β-strand79-80214
α-helix82-10120
β-strand110115
α-helix112-12211
α-helix128-13811
β-strand146115
α-helix148-16821
β-strand176-178313
α-helix180-1867
Chain G: 8 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix45-484
α-helix59-602
α-helix62-687
α-helix69-713
α-helix85-10117
β-strand109-110216
α-helix112-1209
α-helix132-1387
β-strand146-147216
α-helix148-16013
β-strand175117
Chain H: 9 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix27-359
β-strand43118
α-helix45-484
α-helix63-664
α-helix68-714
β-strand80118
α-helix82-9514
β-strand109-110219
α-helix113-1164
α-helix128-1303
α-helix133-1375
β-strand146-147219
α-helix148-16821
β-strand177117

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Programmed cell death protein 6A, B, C, D, E, F, G, Hprotein168Homo sapiensO75340 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>2ZRT_1 Programmed cell death protein 6 (chains A, B, C, D, E, F, G, H)
DQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFS
EFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGR
GQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn37

Primary citation

Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2. Suzuki, H., Kawasaki, M., Kakiuchi, T. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2008) 64:974-977. DOI 10.1107/S1744309108030297 · PubMed

Other PDB entries of the same protein (UniProt O75340 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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