MolNFT v1 · #174301 · protein
Epstein-barr virus, C1 portal-proximal penton vertex, catc binding
7BR7 · Capsid vertex component 2: “Epstein-barr virus, C1 portal-proximal penton vertex, catc binding”. Electron microscopy, 20 pockets (best druggability 0.87). MolNFT v1 #174301 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7BR7
- Type
- protein
- Length
- 9,263 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid vertex component 2; Capsid vertex component 1; Large tegument protein deneddylase…
- EC
- 3.4.19.12, 3.4.22.-
- UniProt
- P03233, P03222, P03186, P14348, P03226, P03187, P25214
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 18 distinct chains · 34% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| K | Capsid vertex component 2 | protein | 68 | 69% helix, 3% strand | P03233 |
| G | Capsid vertex component 2 | protein | 84 | 56% helix, 4% strand | P03233 |
| C | Capsid vertex component 1 | protein | 346 | 29% helix, 20% strand | P03222 |
| B | Large tegument protein deneddylase (EC 3.4.19.12, 3.4.22.-) | protein | 35 | 80% helix, 0% strand | P03186 |
| O | Large tegument protein deneddylase (EC 3.4.19.12, 3.4.22.-) | protein | 29 | 90% helix, 0% strand | P03186 |
| m | Small capsomere-interacting protein | protein | 71 | 44% helix, 0% strand | P14348 |
| Y, Z, 2, y | Small capsomere-interacting protein | protein | 74 | 47% helix, 0% strand | P14348 |
| S | Major capsid protein | protein | 1327 | 34% helix, 15% strand | P03226 |
| T | Major capsid protein | protein | 1305 | 32% helix, 18% strand | P03226 |
| W | Major capsid protein | protein | 1331 | 35% helix, 15% strand | P03226 |
| x | Major capsid protein | protein | 1325 | 33% helix, 15% strand | P03226 |
| e | Triplex capsid protein 1 | protein | 319 | 25% helix, 29% strand | P03187 |
| f | Triplex capsid protein 2 | protein | 290 | 35% helix, 22% strand | P25214 |
| g | Triplex capsid protein 2 | protein | 290 | 31% helix, 17% strand | P25214 |
| l | Major capsid protein | protein | 1250 | 35% helix, 16% strand | P03226 |
| 5 | Triplex capsid protein 1 | protein | 313 | 30% helix, 27% strand | P03187 |
| 6 | Triplex capsid protein 2 | protein | 297 | 34% helix, 19% strand | P25214 |
| 7 | Triplex capsid protein 2 | protein | 287 | 39% helix, 18% strand | P25214 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1011 | 0.87 | 0.88 | 110 | empty |
| 2 | 826 | 0.87 | 0.89 | 101 | empty |
| 3 | 799 | 0.86 | 0.89 | 136 | empty |
| 4 | 979 | 0.86 | 0.88 | 123 | empty |
| 5 | 884 | 0.86 | 0.88 | 77 | empty |
Interfaces
60 interfaces between chains.
- W–x · 6133 Ų buried · 69 hydrogen bonds · protein-protein
- S–T · 5978 Ų buried · 65 hydrogen bonds · protein-protein
- f–g · 3499 Ų buried · 29 hydrogen bonds · protein-protein
- 6–7 · 3299 Ų buried · 25 hydrogen bonds · protein-protein
- S–x · 2412 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 7BR7 · Epstein-Barr virus, C1 portal-proximal penton vertex, CATC binding · the same entry in another collection · chain K against K, 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 P03233
- Every structure of UniProt P03222
- Every structure of UniProt P03186
- Every structure of UniProt P14348
- Every structure of UniProt P03226
- Every structure of UniProt P03187
- Every structure of UniProt P25214
- Elsewhere: RCSB PDB 7BR7 · PDBe 7BR7 · UniProt P03233 · UniProt P03222 · UniProt P03186 · UniProt P14348 · UniProt P03226 · UniProt P03187 · UniProt P25214
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.