MolNFT v1 · #150040 · protein
Structure of lytic transglycosylase mlte inactive mutant E64Q from E.COLI
6GHY · Endo-type membrane-bound lytic murein transglycosylase a: “Structure of lytic transglycosylase mlte inactive mutant E64Q from E.COLI”. X-ray diffraction, 2 pockets (best druggability 0.60). MolNFT v1 #150040 on GenesisL1: 3D…
- PDB
- 6GHY
- Type
- protein
- Length
- 379 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-type membrane-bound lytic murein transglycosylase a
- EC
- 4.2.2.-
- UniProt
- P0C960
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Endo-type membrane-bound lytic murein transglycosylase a (EC 4.2.2.-) | protein | 189 | 64% helix, 3% strand | P0C960 |
| A | Endo-type membrane-bound lytic murein transglycosylase a (EC 4.2.2.-) | protein | 190 | 64% helix, 3% strand | P0C960 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.60 | 0.84 | 26 | empty |
| 2 | 56 | 0.29 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- B–A · 654 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6GHY · Structure of Lytic Transglycosylase MltE inactive mutant E64Q from E.coli · the same entry in another collection · chain B against B, TM-score 1.00
- P0C960 · AlphaFold monomer V2.0 prediction for endo-type membrane-bound lytic murein… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P0C960
- Elsewhere: RCSB PDB 6GHY · PDBe 6GHY · UniProt P0C960
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