2ZRS: Ca2+-bound form of des3-23ALG-2
Crystal structure of Ca2+-bound form of des3-23ALG-2. Determined by X-ray diffraction at 3.1 Å resolution. Released 4 Nov 2008.
- Method
- X-ray diffraction
- Resolution
- 3.1 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 10,956
- Mol. weight
- 159.45 kDa
- Ligands
- CA
- Released
- 4 Nov 2008
Explore 2ZRS in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2ZRS contains 70 α-helices and 32 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: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-33 | 5 | |
| α-helix | 46-49 | 4 | |
| α-helix | 59-61 | 3 | |
| α-helix | 62-69 | 8 | |
| α-helix | 82-88 | 7 | |
| α-helix | 90-100 | 11 | |
| β-strand | 110 | 1 | 1 |
| α-helix | 112-118 | 7 | |
| α-helix | 119-122 | 4 | |
| α-helix | 135-137 | 3 | |
| β-strand | 146 | 1 | 1 |
| α-helix | 152-158 | 7 | |
| α-helix | 164-167 | 4 | |
| α-helix | 183-186 | 4 | |
Chain B: 9 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-33 | 6 | |
| β-strand | 42-43 | 2 | 2 |
| α-helix | 45-48 | 4 | |
| α-helix | 59-61 | 3 | |
| α-helix | 62-71 | 10 | |
| β-strand | 80-81 | 2 | 2 |
| α-helix | 82-102 | 21 | |
| β-strand | 110 | 1 | 3 |
| α-helix | 112-121 | 10 | |
| α-helix | 129-138 | 10 | |
| β-strand | 146 | 1 | 3 |
| α-helix | 148-168 | 21 | |
| α-helix | 180-184 | 5 | |
Chain C: 7 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-35 | 7 | |
| α-helix | 45-51 | 7 | |
| α-helix | 62-70 | 9 | |
| α-helix | 82-100 | 19 | |
| β-strand | 110 | 1 | 4 |
| α-helix | 112-120 | 9 | |
| α-helix | 131-138 | 8 | |
| β-strand | 146 | 1 | 4 |
| α-helix | 148-165 | 18 | |
| β-strand | 175-178 | 4 | 5 |
Chain D: 8 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-35 | 9 | |
| β-strand | 42-43 | 2 | 6 |
| α-helix | 47-51 | 5 | |
| α-helix | 62-70 | 9 | |
| β-strand | 80-81 | 2 | 6 |
| α-helix | 82-102 | 21 | |
| β-strand | 110 | 1 | 7 |
| α-helix | 112-115 | 4 | |
| α-helix | 130-138 | 9 | |
| β-strand | 146 | 1 | 7 |
| α-helix | 148-167 | 20 | |
| β-strand | 176-179 | 4 | 5 |
| α-helix | 180-184 | 5 | |
Chain E: 9 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-35 | 11 | |
| β-strand | 43 | 1 | 8 |
| α-helix | 45-50 | 6 | |
| α-helix | 62-70 | 9 | |
| β-strand | 80 | 1 | 8 |
| α-helix | 82-101 | 20 | |
| α-helix | 113-122 | 10 | |
| α-helix | 128-131 | 4 | |
| α-helix | 134-138 | 5 | |
| α-helix | 148-165 | 18 | |
| β-strand | 175-179 | 5 | 9 |
| α-helix | 180-187 | 8 | |
Chain F: 7 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-35 | 8 | |
| β-strand | 43 | 1 | 10 |
| α-helix | 45-49 | 5 | |
| α-helix | 62-72 | 11 | |
| β-strand | 80 | 1 | 10 |
| α-helix | 82-102 | 21 | |
| β-strand | 110 | 1 | 11 |
| α-helix | 112-120 | 9 | |
| α-helix | 130-138 | 9 | |
| β-strand | 146 | 1 | 11 |
| α-helix | 148-168 | 21 | |
| β-strand | 175-179 | 5 | 9 |
Chain G: 9 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-35 | 9 | |
| β-strand | 43 | 1 | 12 |
| α-helix | 45-51 | 7 | |
| α-helix | 62-72 | 11 | |
| β-strand | 80 | 1 | 12 |
| α-helix | 82-85 | 4 | |
| α-helix | 88-101 | 14 | |
| β-strand | 110 | 1 | 13 |
| α-helix | 112-121 | 10 | |
| α-helix | 130-138 | 9 | |
| β-strand | 146 | 1 | 13 |
| α-helix | 148-161 | 14 | |
| α-helix | 163-166 | 4 | |
| β-strand | 175-177 | 3 | 14 |
Chain H: 9 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 43 | 1 | 15 |
| α-helix | 45-48 | 4 | |
| α-helix | 62-69 | 8 | |
| β-strand | 80 | 1 | 15 |
| α-helix | 82-85 | 4 | |
| α-helix | 93-101 | 9 | |
| β-strand | 110 | 1 | 16 |
| α-helix | 115-121 | 7 | |
| α-helix | 128-131 | 4 | |
| β-strand | 146 | 1 | 16 |
| α-helix | 156-160 | 5 | |
| α-helix | 163-166 | 4 | |
| β-strand | 177-179 | 3 | 14 |
| α-helix | 184-187 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Programmed cell death protein 6 | A, B, C, D, E, F, G, H | protein | 168 | Homo sapiens | O75340 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>2ZRS_1 Programmed cell death protein 6 (chains A, B, C, D, E, F, G, H)
DQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFS
EFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGR
GQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 25 |
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:
- 2ZND 1.7 Å, Crystal structure of Ca2+-free form of des3-20ALG-2
- 2ZNE 2.2 Å, Crystal structure of Zn2+-bound form of des3-23ALG-2 complexed with Alix ABS peptide
- 5GQQ 2.2 Å, Structure of ALG-2/HEBP2 Complex
- 3WXA 2.36 Å, X-ray crystal structural analysis of the complex between ALG-2 and Sec31A peptide
- 2ZN9 2.4 Å, Crystal structure of Ca2+-bound form of des3-20ALG-2
- 3AAJ 2.4 Å, Crystal structure of Ca2+-bound form of des3-23ALG-2deltaGF122
- 2ZN8 2.7 Å, Crystal structure of Zn2+-bound form of ALG-2
- 3AAK 2.7 Å, Crystal structure of Zn2+-bound form of des3-20ALG-2F122A
- 2ZRT 3.3 Å, Crystal structure of Zn2+-bound form of des3-23ALG-2
Browse structure collections
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