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Crystallographic evidence for dual coordination around zinc in the T3R3 human insulin hexamer
Analyse Crystallographic evidence for dual coordination around zinc in the T3R3 human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TRZ
- Type
- protein
- Length
- 102 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
- Ligands
- ZN, NA, CL
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin | protein | 21 | 67% helix, 5% strand | P01308 |
| B, D | Insulin | protein | 30 | 47% helix, 10% strand | P01308 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
- NA · Sodium ion · metal · chains D
- CL · Chloride ion · ion · 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 · 824 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 644 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 614 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 71 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 32 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1TRZ · Crystallographic evidence for dual coordination around zinc in the T3R3 human 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 P01308
- Elsewhere: RCSB PDB 1TRZ · PDBe 1TRZ · UniProt P01308
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