Research workbench
Structure of the FAP7-RPS14 complex
Analyse Structure of the FAP7-RPS14 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CVN
- Type
- protein
- Length
- 1,180 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
- ADP, MG
- Pockets
- 14 · best druggability 0.70
Structure
x-ray diffraction · 8 distinct chains · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative adenylate kinase (EC 2.7.4.3) | protein | 179 | 50% helix, 19% strand | Q9UZK4 |
| B | Putative adenylate kinase (EC 2.7.4.3) | protein | 174 | 52% helix, 17% strand | Q9UZK4 |
| C | Putative adenylate kinase (EC 2.7.4.3) | protein | 179 | 51% helix, 18% strand | Q9UZK4 |
| D | Putative adenylate kinase (EC 2.7.4.3) | protein | 165 | 52% helix, 16% strand | Q9UZK4 |
| E | 30S ribosomal protein S11 | protein | 126 | 30% helix, 29% strand | P62010 |
| F | 30S ribosomal protein S11 | protein | 118 | 30% helix, 33% strand | P62010 |
| G | 30S ribosomal protein S11 | protein | 120 | 29% helix, 34% strand | P62010 |
| H | 30S ribosomal protein S11 | protein | 119 | 32% helix, 30% strand | P62010 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 627 | 0.70 | 0.78 | 60 | empty |
| 2 | 294 | 0.64 | 0.80 | 35 | empty |
| 3 | 394 | 0.60 | 0.77 | 49 | MG |
| 4 | 186 | 0.48 | 0.76 | 27 | empty |
| 5 | 184 | 0.47 | 0.75 | 29 | empty |
Interfaces
11 interfaces between chains.
- C–G · 1859 Ų buried · 35 hydrogen bonds · protein-protein
- B–E · 1819 Ų buried · 39 hydrogen bonds · protein-protein
- D–F · 1809 Ų buried · 38 hydrogen bonds · protein-protein
- A–H · 1796 Ų buried · 38 hydrogen bonds · protein-protein
- A–F · 552 Ų buried · 6 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 4CVN · PDBe 4CVN · UniProt Q9UZK4 · UniProt P62010
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