MolNFT v1 · #14311 · protein
Crystal structure of 2-CO(2+)-insulin at 1.2A resolution
1M5A · Insulin a chain: “Crystal structure of 2-CO(2+)-insulin at 1.2A resolution”. X-ray diffraction, 1 ligand (CO). MolNFT v1 #14311 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1M5A
- Type
- protein
- Length
- 102 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a chain; Insulin B chain
- UniProt
- P01315
- Ligands
- CO
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin a chain | protein | 21 | 67% helix, 14% strand | P01315 |
| B, D | Insulin B chain | protein | 30 | 47% helix, 17% strand | P01315 |
Ligands and binding sites
- CO · Cobalt (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.
- A–B · 900 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 828 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 609 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 58 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 50 Ų buried · 1 hydrogen bond · 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 P01315
- Elsewhere: RCSB PDB 1M5A · PDBe 1M5A · UniProt P01315
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