Research workbench
Insulin with proline analog dfp at position B28 in the R6 state
Analyse Insulin with proline analog dfp at position B28 in the R6 state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UU3
- Type
- protein
- Length
- 572 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin, chain B; Insulin, chain a
- UniProt
- P01308
- Ligands
- IPH, ZN, CL
- Pockets
- 6 · best druggability 0.87
Structure
x-ray diffraction · 9 distinct chains · 67% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin, chain B | protein | 19 | 58% helix, 0% strand | P01308 |
| B, D, N, P, R, V | Insulin, chain a | protein | 27 | 74% helix, 11% strand | P01308 |
| C, E, G | Insulin, chain B | protein | 20 | 50% helix, 0% strand | P01308 |
| F | Insulin, chain a | protein | 26 | 77% helix, 12% strand | P01308 |
| H, L, T | Insulin, chain a | protein | 28 | 75% helix, 11% strand | P01308 |
| I, K, M, O, Q, S, U | Insulin, chain B | protein | 21 | 57% helix, 5% strand | P01308 |
| J | Insulin, chain a | protein | 28 | 71% helix, 11% strand | P01308 |
| W | Insulin, chain B | protein | 20 | 55% helix, 5% strand | P01308 |
| X | Insulin, chain a | protein | 26 | 73% helix, 12% strand | P01308 |
Ligands and binding sites
- IPH · Phenol · ligand · 11 copies · chains A, B, F, H, C, D, L, E, J, G, I, K, M, N, R, T, Q, V, X, P, S, U, W
- ZN · Zinc ion · metal · 4 copies · chains B, F, J, D, H, L, N, R, V, P, T, X
- CL · Chloride ion · ion · 4 copies · chains D, H, L, B, F, J, N, R, V, P, T, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1162 | 0.87 | 0.87 | 172 | IPH |
| 2 | 1108 | 0.86 | 0.87 | 147 | IPH, CL |
| 3 | 55 | 0.61 | 0.92 | 18 | IPH |
| 4 | 182 | 0.49 | 0.76 | 40 | empty |
| 5 | 58 | 0.36 | 0.78 | 14 | empty |
Interfaces
67 interfaces between chains.
- J–L · 691 Ų buried · 10 hydrogen bonds · protein-protein
- V–X · 691 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 690 Ų buried · 9 hydrogen bonds · protein-protein
- R–T · 689 Ų buried · 14 hydrogen bonds · protein-protein
- N–P · 685 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 disulfide, 11 modified (disulfide, nonstandard).
Compared structures
- 5UU3 · Insulin with proline analog DfP at position B28 in the R6 state · the same entry in another collection · chain I against I, TM-score 1.00
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 P01308
- Elsewhere: RCSB PDB 5UU3 · PDBe 5UU3 · UniProt P01308
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