Research workbench
Local refinement of RHAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex
Analyse Local refinement of RHAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V0S
- Type
- protein
- Length
- 1,315 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Blood group RH(CE) polypeptide; Ammonium transporter rh type a; Ankyrin-1
- UniProt
- P18577, Q02094, P16157
- Ligands
- CLR, AJP
- Pockets
- 19 · best druggability 0.78
Structure
electron microscopy · 4 distinct chains · 70% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| K | Blood group RH(CE) polypeptide | protein | 380 | 71% helix, 2% strand | P18577 |
| L | Ammonium transporter rh type a | protein | 388 | 72% helix, 2% strand | Q02094 |
| Q | Ammonium transporter rh type a | protein | 390 | 73% helix, 2% strand | Q02094 |
| J | Ankyrin-1 | protein | 157 | 57% helix, 1% strand | P16157 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.78 | 0.98 | 21 | empty |
| 2 | 348 | 0.73 | 0.84 | 51 | empty |
| 3 | 664 | 0.69 | 0.77 | 51 | empty |
| 4 | 201 | 0.63 | 0.83 | 40 | empty |
| 5 | 315 | 0.62 | 0.79 | 41 | empty |
Interfaces
6 interfaces between chains.
- K–L · 2869 Ų buried · 24 hydrogen bonds · protein-protein
- L–Q · 2691 Ų buried · 33 hydrogen bonds · protein-protein
- K–Q · 2553 Ų buried · 12 hydrogen bonds · protein-protein
- K–J · 1036 Ų buried · 22 hydrogen bonds · protein-protein
- Q–J · 70 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7V0S · Local refinement of RhAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex · the same entry in another collection · chain J against J, TM-score 1.00
- Q02094 · AlphaFold monomer V2.0 prediction for ammonium transporter rh type a (Q02094) · a predicted model of the same protein · chain L against A, TM-score 1.00
- P16157 · AlphaFold monomer V2.0 prediction for ankyrin-1 (P16157) · a predicted model of the same protein · chain J against A, TM-score 0.99
- P18577 · AlphaFold monomer V2.0 prediction for blood group RH(CE) polypeptide (P18577) · a predicted model of the same protein · chain K against A, TM-score 0.96
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P18577
- Every structure of UniProt Q02094
- Every structure of UniProt P16157
- Elsewhere: RCSB PDB 7V0S · PDBe 7V0S · UniProt P18577 · UniProt Q02094 · UniProt P16157
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