Research workbench
Crystal structure of the uncharacterized maf protein ycef from E. COLI
Analyse Crystal structure of the uncharacterized maf protein ycef from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JHC
- Type
- protein
- Length
- 374 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maf-like protein ycef
- UniProt
- P0A729
- Ligands
- UNX
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maf-like protein ycef | protein | 192 | 34% helix, 27% strand | P0A729 |
| B | Maf-like protein ycef | protein | 182 | 34% helix, 29% strand | P0A729 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 12 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.58 | 0.82 | 24 | empty |
| 2 | 321 | 0.57 | 0.76 | 30 | GOL |
| 3 | 229 | 0.55 | 0.78 | 27 | GOL, UNX |
Interfaces
1 interface between chains.
- A–B · 1434 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 4JHC · Crystal structure of the uncharacterized Maf protein YceF from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0A729 · AlphaFold monomer V2.0 prediction for 7-methyl-GTP pyrophosphatase (P0A729) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P0A729
- Elsewhere: RCSB PDB 4JHC · PDBe 4JHC · UniProt P0A729
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