MolNFT v1 · #14623 · protein
Crystal structure of human calcineurin complexed with cyclosporin a and human cyclophilin
1MF8 · Calmodulin-dependent calcineurin a subunit, alpha isoform: “Crystal structure of human calcineurin complexed with cyclosporin a and human cyclophilin”. X-ray diffraction, 2 ligands (CA, PO4), 6 pockets (best druggability 0.74).…
- PDB
- 1MF8
- Type
- protein
- Length
- 691 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin-dependent calcineurin a subunit, alpha isoform; Calcineurin B subunit isoform…
- EC
- 3.1.3.16, 5.2.1.8
- UniProt
- Q08209, P63098, P62937
- Ligands
- CA, PO4
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin-dependent calcineurin a subunit, alpha isoform (EC 3.1.3.16) | protein | 352 | 37% helix, 17% strand | Q08209 |
| B | Calcineurin B subunit isoform 1 (EC 3.1.3.16) | protein | 164 | 57% helix, 5% strand | P63098 |
| C | Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8) | protein | 164 | 14% helix, 34% strand | P62937 |
| D | Cyclosporin a | protein | 11 | 0% helix, 9% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 686 | 0.74 | 0.80 | 79 | empty |
| 2 | 263 | 0.65 | 0.82 | 38 | empty |
| 3 | 517 | 0.64 | 0.76 | 42 | PO4 |
| 4 | 104 | 0.61 | 0.87 | 18 | empty |
| 5 | 80 | 0.38 | 0.78 | 19 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1945 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 503 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 415 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 411 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 222 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 1 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 1MF8 · Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin · the same entry in another collection · chain A against A, TM-score 1.00
- Q08209 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 2B catalytic… · a predicted model of the same protein · chain A against A, TM-score 0.96
- P63098 · AlphaFold monomer V2.0 prediction for calcineurin subunit B type 1 (P63098) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q08209
- Every structure of UniProt P63098
- Every structure of UniProt P62937
- Elsewhere: RCSB PDB 1MF8 · PDBe 1MF8 · UniProt Q08209 · UniProt P63098 · UniProt P62937
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.