MolNFT v1 · #102352 · protein
Crystal structure of a putative tailspike protein (TSP1, ORF210) from escherichia COLI O157:H7 bacteriohage CBA120
4OJ5: “Crystal structure of a putative tailspike protein (TSP1, ORF210) from escherichia COLI O157:H7 bacteriohage…”. X-ray diffraction, 1 ligand (ZN), 19 pockets (best druggability 0.90). MolNFT v1 #102352 on GenesisL1: 3D structure…
- PDB
- 4OJ5
- Type
- protein
- Length
- 2,271 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tailspike protein
- UniProt
- G3M189
- Ligands
- ZN
- Pockets
- 19 · best druggability 0.90
Structure
x-ray diffraction · 3 distinct chains · 12% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tailspike protein | protein | 758 | 12% helix, 38% strand | G3M189 |
| B | Tailspike protein | protein | 756 | 12% helix, 38% strand | G3M189 |
| C | Tailspike protein | protein | 757 | 12% helix, 38% strand | G3M189 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1128 | 0.90 | 0.92 | 148 | empty |
| 2 | 1151 | 0.85 | 0.86 | 92 | empty |
| 3 | 802 | 0.70 | 0.76 | 89 | empty |
| 4 | 62 | 0.69 | 0.96 | 27 | empty |
| 5 | 463 | 0.60 | 0.75 | 62 | empty |
Interfaces
3 interfaces between chains.
- A–C · 3772 Ų buried · 48 hydrogen bonds · protein-protein
- B–C · 3764 Ų buried · 51 hydrogen bonds · protein-protein
- A–B · 3729 Ų buried · 48 hydrogen bonds · protein-protein
Compared structures
- 4OJ5 · Crystal Structure of a Putative Tailspike Protein (TSP1, orf210) from Escherichia coli… · the same entry in another collection · chain A against A, TM-score 1.00
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 G3M189
- Elsewhere: RCSB PDB 4OJ5 · PDBe 4OJ5 · UniProt G3M189
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