MolNFT v1 · #29921 · protein
INSULIN
1ZNI: “INSULIN”. X-ray diffraction, 2 ligands (ZN, CL). MolNFT v1 #29921 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ZNI
- Type
- protein
- Length
- 102 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01315
- Ligands
- ZN, CL
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin | protein | 21 | 57% helix, 5% strand | P01315 |
| B, D | Insulin | protein | 30 | 63% helix, 10% strand | P01315 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- C–D · 825 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 662 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 659 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 60 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 32 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1ZNI · INSULIN · 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 P01315
- Elsewhere: RCSB PDB 1ZNI · PDBe 1ZNI · UniProt P01315
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