MolNFT v1 · #95430 · protein
P21 crystal form of FKBP12.6
4IQ2 · Peptidyl-prolyl cis-trans isomerase FKBP1B: “P21 crystal form of FKBP12.6”. X-ray diffraction, 1 pocket (best druggability 0.33). MolNFT v1 #95430 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4IQ2
- Type
- protein
- Length
- 214 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP1B
- EC
- 5.2.1.8
- UniProt
- P68106
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peptidyl-prolyl cis-trans isomerase FKBP1B (EC 5.2.1.8) | protein | 107 | 9% helix, 38% strand | P68106 |
Ligands and binding sites
- MLA · Malonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.33 | 0.77 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 497 Ų buried · 5 hydrogen bonds · protein-protein
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 P68106
- Elsewhere: RCSB PDB 4IQ2 · PDBe 4IQ2 · UniProt P68106
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