Research workbench
Crystal structure of alpha-hemolysin
Analyse Crystal structure of alpha-hemolysin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ANZ
- Type
- protein
- Length
- 8,243 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-hemolysin
- UniProt
- Q99UU6
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, K, M, O, S, U, V, b | Alpha-hemolysin | protein | 295 | 5% helix, 59% strand | Q99UU6 |
| C, F, G, H, I, J, L, N, P, Q, R, T, W, X, Y, Z, a | Alpha-hemolysin | protein | 294 | 5% helix, 59% strand | Q99UU6 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 56 copies · chains A, F, G, B, C, D, E, H, M, N, I, J, K, L, O, T, U, P, Q, R, S, V, a, b, W, X, Y, Z
- ACY · Acetic acid · additive · 28 copies · chains A, G, B, C, D, E, F, H, N, I, J, K, L, M, O, U, P, Q, R, S, T, V, W, X, Y, Z, a, b
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 757 | 0.81 | 0.85 | 112 | MPD |
| 2 | 984 | 0.81 | 0.82 | 110 | MPD |
| 3 | 1062 | 0.80 | 0.82 | 116 | MPD |
| 4 | 711 | 0.80 | 0.84 | 103 | MPD |
| 5 | 415 | 0.75 | 0.85 | 61 | MPD |
Interfaces
71 interfaces between chains.
- Y–Z · 3001 Ų buried · 65 hydrogen bonds · protein-protein
- W–X · 2988 Ų buried · 67 hydrogen bonds · protein-protein
- F–G · 2988 Ų buried · 66 hydrogen bonds · protein-protein
- B–C · 2981 Ų buried · 67 hydrogen bonds · protein-protein
- H–N · 2979 Ų buried · 65 hydrogen bonds · protein-protein
Compared structures
- 3ANZ · Crystal Structure of alpha-hemolysin · the same entry in another collection · chain E against E, 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 Q99UU6
- Elsewhere: RCSB PDB 3ANZ · PDBe 3ANZ · UniProt Q99UU6
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