Research workbench
Crystal structure of brucella abortus plic in complex with human lysozyme
Analyse Crystal structure of brucella abortus plic in complex with human lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ML7
- Type
- protein
- Length
- 455 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme C; Humanlysozyme
- EC
- 3.2.1.17
- UniProt
- P61626
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme C (EC 3.2.1.17) | protein | 129 | 40% helix, 12% strand | P61626 |
| B, D | Humanlysozyme | protein | 98 | 0% helix, 62% strand | — |
| C | Lysozyme C (EC 3.2.1.17) | protein | 130 | 38% helix, 12% strand | P61626 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.78 | 0.91 | 31 | empty |
| 2 | 107 | 0.44 | 0.78 | 19 | empty |
| 3 | 80 | 0.35 | 0.76 | 19 | empty |
| 4 | 78 | 0.35 | 0.76 | 17 | empty |
| 5 | 52 | 0.26 | 0.73 | 14 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1634 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1151 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 1131 Ų buried · 28 hydrogen bonds · protein-protein
- B–C · 356 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 321 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 4ML7 · Crystal structure of Brucella abortus PliC in complex with human lysozyme · 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 P61626
- Elsewhere: RCSB PDB 4ML7 · PDBe 4ML7 · UniProt P61626
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.