Crystallographic refinement of ricin to 2.5 Angstroms. Determined by X-ray diffraction at 2.5 Å resolution. Released 31 Jan 1994.
Explore 2AAI in 3D Show helices and sheets RCSB PDB PDBe
2AAI contains 25 α-helices and 47 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 | 8-12 | 5 | 1 |
| α-helix | 18-32 | 15 | |
| β-strand | 38-39 | 2 | 2 |
| β-strand | 42-43 | 2 | 2 |
| β-strand | 44 | 1 | 3 |
| α-helix | 45-47 | 3 | |
| β-strand | 57-63 | 7 | 1 |
| β-strand | 69-75 | 7 | 1 |
| β-strand | 80-86 | 7 | 1 |
| β-strand | 89-92 | 4 | 1 |
| α-helix | 98-104 | 7 | |
| β-strand | 113-116 | 4 | 1 |
| α-helix | 123-130 | 8 | |
| β-strand | 139 | 1 | 4 |
| α-helix | 141-156 | 16 | |
| α-helix | 161-180 | 20 | |
| α-helix | 182-194 | 13 | |
| β-strand | 198 | 1 | 4 |
| α-helix | 199-201 | 3 | |
| α-helix | 202-219 | 18 | |
| β-strand | 230-231 | 2 | 5 |
| β-strand | 241-242 | 2 | 5 |
| β-strand | 255 | 1 | 3 |
| β-strand | 260 | 1 | 6 |
| α-helix | 261 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 6 |
| β-strand | 10-11 | 2 | 7 |
| β-strand | 13-14 | 2 | 8 |
| α-helix | 16-18 | 3 | |
| α-helix | 19 | 1 | |
| β-strand | 20-23 | 4 | 8 |
| α-helix | 24-26 | 3 | |
| α-helix | 32 | 1 | |
| β-strand | 33 | 1 | 7 |
| β-strand | 34-37 | 4 | 8 |
| α-helix | 45-47 | 3 | |
| β-strand | 49-51 | 3 | 7 |
| β-strand | 56 | 1 | 9 |
| β-strand | 57-59 | 3 | 7 |
| β-strand | 62-66 | 5 | 7 |
| β-strand | 74 | 1 | 10 |
| β-strand | 75-79 | 5 | 7 |
| α-helix | 85-87 | 3 | |
| β-strand | 89 | 1 | 9 |
| β-strand | 91-92 | 2 | 10 |
| β-strand | 98-101 | 4 | 10 |
| β-strand | 104-108 | 5 | 10 |
| α-helix | 116 | 1 | |
| β-strand | 117 | 1 | 8 |
| α-helix | 118 | 1 | |
| β-strand | 119-122 | 4 | 10 |
| α-helix | 127-129 | 3 | |
| β-strand | 132-133 | 2 | 8 |
| α-helix | 139 | 1 | |
| β-strand | 140-142 | 3 | 11 |
| β-strand | 143-145 | 3 | 12 |
| α-helix | 147-149 | 3 | |
| α-helix | 150 | 1 | |
| β-strand | 151-155 | 5 | 12 |
| β-strand | 158-162 | 5 | 12 |
| β-strand | 173-175 | 3 | 11 |
| β-strand | 181-183 | 3 | 11 |
| β-strand | 189-193 | 5 | 12 |
| β-strand | 202-206 | 5 | 12 |
| β-strand | 217-218 | 2 | 13 |
| β-strand | 224-225 | 2 | 13 |
| β-strand | 232-235 | 4 | 13 |
| α-helix | 236-238 | 3 | |
| α-helix | 240-242 | 3 | |
| β-strand | 245-248 | 4 | 13 |
| α-helix | 254-256 | 3 | |
| β-strand | 259-261 | 3 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ricin (a chain) | A | protein | 267 | Ricinus communis | P02879 (AlphaFold model) |
| Ricin (B chain) | B | protein | 262 | P02879 (AlphaFold model) |
>2AAI_1 RICIN (A CHAIN) (chains A) IFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILV ELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFG GNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQLPTLARSFIICIQMISEAAR FQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKF SVYDVSILIPIIALMVYRCAPPPSSQF
>2AAI_2 RICIN (B CHAIN) (chains B) ADVCMDPEPIVRIVGRNGLCVDVRDGRFHNGNAIQLWPCKSNTDANQLWTLKRDNTIRSN GKCLTTYGYSPGVYVMIYDCNTAATDATRWQIWDNGTIINPRSSLVLAATSGNSGTTLTV QTNIYAVSQGWLPTNNTQPFVTTIVGLYGLCLQANSGQVWIEDCSSEKAEQQWALYADGS IRPQQNRDNCLTSDSNIRETVVKILSCGPASSGQRWMFKNDGTILNLYSGLVLDVRASDP SLKQIILYPLHGDPNQIWLPLF
Crystallographic refinement of ricin to 2.5 A. Rutenber, E., Katzin, B.J., Ernst, S. et al. Proteins (1991) 10:240-250. DOI 10.1002/prot.340100308 · PubMed
Other PDB entries of the same protein (UniProt P02879 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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