MolNFT v1 · #113814 · protein
Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues
5AQP · Heat shock cognate 71 kda protein: “Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues”. X-ray diffraction, 1 ligand (1LQ), 14 pockets (best druggability 0.73). MolNFT v1 #113814 on…
- PDB
- 5AQP
- Type
- protein
- Length
- 1,478 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock cognate 71 kda protein; Bag family molecular chaperone regulator 1
- EC
- 3.6.3.51
- UniProt
- P11142, Q99933
- Ligands
- 1LQ
- Pockets
- 14 · best druggability 0.73
Structure
x-ray diffraction · 5 distinct chains · 51% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock cognate 71 kda protein (EC 3.6.3.51) | protein | 382 | 38% helix, 29% strand | P11142 |
| B | Bag family molecular chaperone regulator 1 | protein | 111 | 79% helix, 0% strand | Q99933 |
| C, E | Heat shock cognate 71 kda protein (EC 3.6.3.51) | protein | 381 | 39% helix, 29% strand | P11142 |
| D | Bag family molecular chaperone regulator 1 | protein | 111 | 80% helix, 0% strand | Q99933 |
| F | Bag family molecular chaperone regulator 1 | protein | 112 | 80% helix, 0% strand | Q99933 |
Ligands and binding sites
- 1LQ · quinazolin-4-amine · ligand · 3 copies · chains A, C, E
- GOL · Glycerol · additive · 14 copies · chains A, B, C, D, E, F
- DMS · Dimethyl sulfoxide · additive · 5 copies · chains A, C, E
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1184 | 0.73 | 0.76 | 93 | GOL |
| 2 | 793 | 0.72 | 0.78 | 72 | 1LQ, DMS, TRS |
| 3 | 772 | 0.71 | 0.77 | 71 | 1LQ, GOL, DMS, TRS |
| 4 | 589 | 0.68 | 0.78 | 53 | 1LQ, GOL |
| 5 | 275 | 0.53 | 0.75 | 27 | empty |
Interfaces
9 interfaces between chains.
- E–F · 968 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 953 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 952 Ų buried · 28 hydrogen bonds · protein-protein
- A–F · 211 Ų buried · 3 hydrogen bonds · protein-protein
- B–F · 169 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 5AQP · Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site… · the same entry in another collection · chain F against F, TM-score 1.00
- Q99933 · AlphaFold monomer V2.0 prediction for bag family molecular chaperone regulator 1 (Q99933) · a predicted model of the same protein · chain D against A, TM-score 0.93
- P11142 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P11142) · a predicted model of the same protein · chain C against A, TM-score 0.83
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 P11142
- Every structure of UniProt Q99933
- Elsewhere: RCSB PDB 5AQP · PDBe 5AQP · UniProt P11142 · UniProt Q99933
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