Research workbench
Structure of murj from escherichia COLI
Analyse Structure of murj from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CC4
- Type
- protein
- Length
- 608 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble cytochrome B562, lipid II flippase murj chimera
- UniProt
- P0ABE7, P0AF16
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Soluble cytochrome B562, lipid II flippase murj chimera | protein | 608 | 82% helix, 0% strand | P0ABE7, P0AF16 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
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 | 915 | 0.79 | 0.81 | 98 | empty |
| 2 | 862 | 0.72 | 0.76 | 72 | empty |
| 3 | 81 | 0.49 | 0.82 | 17 | empty |
| 4 | 117 | 0.43 | 0.77 | 18 | empty |
| 5 | 107 | 0.38 | 0.74 | 18 | empty |
Compared structures
- 6CC4 · Structure of MurJ from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0AF16 · AlphaFold monomer V2.0 prediction for lipid II flippase murj (P0AF16) · a predicted model of the same protein · chain A against A, TM-score 0.80
- P0ABE7 · AlphaFold monomer V2.0 prediction for soluble cytochrome B562 (P0ABE7) · a predicted model of the same protein · chain A against A, TM-score 0.17
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 P0ABE7
- Every structure of UniProt P0AF16
- Elsewhere: RCSB PDB 6CC4 · PDBe 6CC4 · UniProt P0ABE7 · UniProt P0AF16
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