MolNFT v1 · #99473 · protein
Radiation damage study of cu T6-insulin - 0.12 mgy
4M4I: “Radiation damage study of cu T6-insulin - 0.12 mgy”. X-ray diffraction, 1 ligand (CU). MolNFT v1 #99473 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4M4I
- Type
- protein
- Length
- 101 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01317
- Ligands
- CU
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin | protein | 21 | 57% helix, 10% strand | P01317 |
| B | Insulin | protein | 29 | 48% helix, 14% strand | P01317 |
| D | Insulin | protein | 30 | 47% helix, 13% strand | P01317 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- C–D · 908 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 906 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 653 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 70 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 45 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 4M4I · Radiation damage study of Cu T6-insulin - 0.12 MGy · the same entry in another collection · chain A against A, 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 P01317
- Elsewhere: RCSB PDB 4M4I · PDBe 4M4I · UniProt P01317
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