MolNFT v2 · #5 · protein
102L: How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme
102L: “How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme”. X-ray diffraction at 1.74, 1 ligand (CL), 1 pocket (best druggability 0.52). MolNFT v2 #5 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 102L
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Authors
- Heinz, D.W., Matthews, B.W.
- Deposited
- 09/29/92
- Collection
- MolNFT
- Contract
- 0x08363bae41CBeD54a47FC1e6eeE29bf6f00Cb2ba
- Owner
- 0xF80704d7b5fE70cd0C222aD976c42d16A10fdfeA
- Resolution
- 1.74
- Source
- Enterobacteria phage T4
- Molecule
- T4 lysozyme
- UniProt
- P00720
- Ligands
- CL
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · resolution 1.74 · 1 distinct chain · 66% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T4 lysozyme | protein | 163 | 66% helix, 9% strand | P00720 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.52 | 0.75 | 30 | empty |
Compared structures
- 102L · How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme · the same entry in another collection · chain A against A, TM-score 1.00
- 102L · How amino-acid insertions are allowed in an alpha-helix of T4 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 P00720
- Elsewhere: RCSB PDB 102L · PDBe 102L · UniProt P00720
Other records of 102L
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