MolNFT v1 · #172360 · protein
Bacillus endospore appendages form a novel family of disulfide-linked pili
7A02 · DUF3992 domain-containing protein: “Bacillus endospore appendages form a novel family of disulfide-linked pili”. Electron microscopy, 20 pockets (best druggability 0.78). MolNFT v1 #172360 on GenesisL1: 3D structure, binding sites…
- PDB
- 7A02
- Type
- protein
- Length
- 2,576 residues
- Chains
- 23
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DUF3992 domain-containing protein
- UniProt
- A0A1Y6A695
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 0% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W | DUF3992 domain-containing protein | protein | 112 | 0% helix, 59% strand | A0A1Y6A695 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.78 | 0.86 | 63 | empty |
| 2 | 275 | 0.76 | 0.89 | 52 | empty |
| 3 | 394 | 0.72 | 0.83 | 42 | empty |
| 4 | 261 | 0.71 | 0.86 | 36 | empty |
| 5 | 226 | 0.69 | 0.86 | 35 | empty |
Interfaces
61 interfaces between chains.
- R–S · 1092 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 1090 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1076 Ų buried · 10 hydrogen bonds · protein-protein
- T–W · 1072 Ų buried · 12 hydrogen bonds · protein-protein
- M–N · 1066 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 26 disulfide (disulfide).
Compared structures
- 7A02 · Bacillus endospore appendages form a novel family of disulfide-linked pili · the same entry in another collection · chain G against G, 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 A0A1Y6A695
- Elsewhere: RCSB PDB 7A02 · PDBe 7A02 · UniProt A0A1Y6A695
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