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Crystal structure of ylib protein from escherichia coi
Analyse Crystal structure of ylib protein from escherichia coi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UQW
- Type
- protein
- Length
- 974 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative binding protein ylib
- UniProt
- P75797
- Ligands
- ZN
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative binding protein ylib | protein | 487 | 32% helix, 26% strand | P75797 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.76 | 0.91 | 41 | GOL |
| 2 | 182 | 0.75 | 0.92 | 34 | empty |
| 3 | 762 | 0.68 | 0.75 | 74 | empty |
| 4 | 774 | 0.67 | 0.75 | 79 | empty |
| 5 | 88 | 0.37 | 0.75 | 18 | GOL |
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
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 P75797
- Elsewhere: RCSB PDB 1UQW · PDBe 1UQW · UniProt P75797
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