MolNFT v1 · #181954 · protein
Crystal structure of TNSC(1-503)A225V
7MBW · Transposon TN7 transposition protein tnsc: “Crystal structure of TNSC(1-503)A225V”. X-ray diffraction, 2 ligands (ADP, MG), 20 pockets (best druggability 0.76). MolNFT v1 #181954 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 7MBW
- Type
- protein
- Length
- 1,872 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transposon TN7 transposition protein tnsc
- UniProt
- P05846
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transposon TN7 transposition protein tnsc | protein | 475 | 55% helix, 9% strand | P05846 |
| B | Transposon TN7 transposition protein tnsc | protein | 469 | 56% helix, 8% strand | P05846 |
| C | Transposon TN7 transposition protein tnsc | protein | 461 | 57% helix, 9% strand | P05846 |
| D | Transposon TN7 transposition protein tnsc | protein | 467 | 57% helix, 9% strand | P05846 |
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
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 850 | 0.76 | 0.80 | 94 | ADP, MG |
| 2 | 362 | 0.75 | 0.86 | 42 | empty |
| 3 | 638 | 0.74 | 0.81 | 61 | empty |
| 4 | 525 | 0.74 | 0.82 | 43 | empty |
| 5 | 574 | 0.73 | 0.80 | 65 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2441 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 2353 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 1563 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 94 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 13 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 44 modified (engineered).
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 P05846
- Elsewhere: RCSB PDB 7MBW · PDBe 7MBW · UniProt P05846
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