Research workbench
Structure of the FAP7-RPS14 complex in complex with ATP
Analyse Structure of the FAP7-RPS14 complex in complex with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CW7
- Type
- protein
- Length
- 1,191 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative adenylate kinase; 30S ribosomal protein S11
- EC
- 2.7.4.3
- UniProt
- Q9UZK4, P62010
- Ligands
- ATP, ADP, MG
- Pockets
- 15 · best druggability 0.69
Structure
x-ray diffraction · 8 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative adenylate kinase (EC 2.7.4.3) | protein | 181 | 49% helix, 19% strand | Q9UZK4 |
| B | 30S ribosomal protein S11 | protein | 118 | 30% helix, 34% strand | P62010 |
| C | Putative adenylate kinase (EC 2.7.4.3) | protein | 172 | 52% helix, 17% strand | Q9UZK4 |
| D | 30S ribosomal protein S11 | protein | 120 | 29% helix, 31% strand | P62010 |
| E | Putative adenylate kinase (EC 2.7.4.3) | protein | 180 | 49% helix, 16% strand | Q9UZK4 |
| F | 30S ribosomal protein S11 | protein | 118 | 33% helix, 31% strand | P62010 |
| G | Putative adenylate kinase (EC 2.7.4.3) | protein | 180 | 49% helix, 18% strand | Q9UZK4 |
| H | 30S ribosomal protein S11 | protein | 122 | 29% helix, 30% strand | P62010 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B, E, F
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains C, G
- MG · Magnesium ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 443 | 0.69 | 0.80 | 50 | ATP, MG |
| 2 | 401 | 0.68 | 0.81 | 54 | empty |
| 3 | 438 | 0.68 | 0.80 | 54 | empty |
| 4 | 439 | 0.68 | 0.80 | 43 | empty |
| 5 | 430 | 0.65 | 0.78 | 48 | empty |
Interfaces
14 interfaces between chains.
- E–F · 1862 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 1825 Ų buried · 37 hydrogen bonds · protein-protein
- G–H · 1793 Ų buried · 35 hydrogen bonds · protein-protein
- C–D · 1724 Ų buried · 34 hydrogen bonds · protein-protein
- D–F · 774 Ų buried · 4 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 Q9UZK4
- Every structure of UniProt P62010
- Elsewhere: RCSB PDB 4CW7 · PDBe 4CW7 · UniProt Q9UZK4 · UniProt P62010
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