MolNFT v1 · #20651 · protein
Retinol binding protein complexed with transthyretin
1RLB: “Retinol binding protein complexed with transthyretin”. X-ray diffraction, 1 ligand (REA), 9 pockets (best druggability 0.84). MolNFT v1 #20651 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RLB
- Type
- protein
- Length
- 834 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin; Retinol binding protein
- UniProt
- P02766, P02753
- Ligands
- REA
- Pockets
- 9 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 7% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Transthyretin | protein | 123 | 5% helix, 49% strand | P02766 |
| B, D | Transthyretin | protein | 120 | 4% helix, 45% strand | P02766 |
| E, F | Retinol binding protein | protein | 174 | 11% helix, 42% strand | P02753 |
Ligands and binding sites
- REA · Retinoic acid · ligand · 2 copies · chains B, E, A, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.84 | 0.96 | 29 | REA |
| 2 | 186 | 0.83 | 0.97 | 30 | REA |
| 3 | 610 | 0.75 | 0.82 | 68 | empty |
| 4 | 323 | 0.71 | 0.84 | 40 | empty |
| 5 | 222 | 0.59 | 0.80 | 44 | empty |
Interfaces
12 interfaces between chains.
- A–B · 928 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 874 Ų buried · 17 hydrogen bonds · protein-protein
- A–F · 391 Ų buried · 4 hydrogen bonds · protein-protein
- B–E · 383 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 371 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P02766
- Every structure of UniProt P02753
- Elsewhere: RCSB PDB 1RLB · PDBe 1RLB · UniProt P02766 · UniProt P02753
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