MolNFT v1 · #153090 · protein
ATFKBP53 N-terminal nucleoplasmin domain
6J2Z · Peptidyl-prolyl cis-trans isomerase FKBP53: “ATFKBP53 N-terminal nucleoplasmin domain”. X-ray diffraction, 11 pockets (best druggability 0.82). MolNFT v1 #153090 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6J2Z
- Type
- protein
- Length
- 937 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP53
- EC
- 5.2.1.8
- UniProt
- Q93ZG9
- Pockets
- 11 · best druggability 0.82
Structure
x-ray diffraction · 5 distinct chains · 2% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Peptidyl-prolyl cis-trans isomerase FKBP53 (EC 5.2.1.8) | protein | 82 | 0% helix, 54% strand | Q93ZG9 |
| G | Peptidyl-prolyl cis-trans isomerase FKBP53 (EC 5.2.1.8) | protein | 88 | 0% helix, 58% strand | Q93ZG9 |
| H, I, A, C, D, E | Peptidyl-prolyl cis-trans isomerase FKBP53 (EC 5.2.1.8) | protein | 96 | 3% helix, 55% strand | Q93ZG9 |
| J | Peptidyl-prolyl cis-trans isomerase FKBP53 (EC 5.2.1.8) | protein | 94 | 3% helix, 54% strand | Q93ZG9 |
| B | Peptidyl-prolyl cis-trans isomerase FKBP53 (EC 5.2.1.8) | protein | 97 | 3% helix, 58% strand | Q93ZG9 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 841 | 0.82 | 0.84 | 80 | empty |
| 2 | 344 | 0.79 | 0.89 | 48 | empty |
| 3 | 502 | 0.69 | 0.79 | 35 | empty |
| 4 | 478 | 0.69 | 0.80 | 39 | empty |
| 5 | 160 | 0.58 | 0.82 | 24 | empty |
Interfaces
12 interfaces between chains.
- A–B · 909 Ų buried · 11 hydrogen bonds · protein-protein
- H–I · 903 Ų buried · 10 hydrogen bonds · protein-protein
- I–J · 898 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 897 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 889 Ų buried · 13 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 Q93ZG9
- Elsewhere: RCSB PDB 6J2Z · PDBe 6J2Z · UniProt Q93ZG9
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