Research workbench
Structure of the 2TEL crystallization module fused to T4 lysozyme with an ala-gly-pro linker.
Analyse Structure of the 2TEL crystallization module fused to T4 lysozyme with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QB0
- Type
- protein
- Length
- 636 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E80-telsam domain; Telsam domain - lysozyme chimera
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- MN
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | E80-telsam domain | protein | 77 | 58% helix, 0% strand | — |
| B, D | Telsam domain - lysozyme chimera (EC 3.2.1.17) | protein | 241 | 60% helix, 6% strand | P00720 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 5 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.61 | 0.83 | 23 | empty |
| 2 | 192 | 0.60 | 0.82 | 24 | empty |
| 3 | 239 | 0.48 | 0.74 | 25 | MN |
| 4 | 152 | 0.43 | 0.74 | 20 | empty |
| 5 | 173 | 0.43 | 0.74 | 27 | MN |
Interfaces
3 interfaces between chains.
- A–D · 711 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 708 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 324 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2QB0 · Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro… · 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 P00720
- Elsewhere: RCSB PDB 2QB0 · PDBe 2QB0 · UniProt P00720
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