Research workbench
Crystal structure of rb human arg-insulin
Analyse Crystal structure of rb human arg-insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R35
- Type
- protein
- Length
- 101 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
- Ligands
- RB, NA
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin | protein | 22 | 45% helix, 0% strand | P01308 |
| B | Insulin | protein | 28 | 54% helix, 7% strand | P01308 |
| C | Insulin | protein | 21 | 19% helix, 5% strand | P01308 |
| D | Insulin | protein | 30 | 33% helix, 10% strand | P01308 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
4 interfaces between chains.
- C–D · 855 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 599 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 587 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 48 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2R35 · Crystal structure of RB human arg-insulin · the same entry in another collection · chain B against B, 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 2R35 · PDBe 2R35 · UniProt P01308
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