Research workbench
Native crystal structure of mltf pseudomonas aeruginosa
Analyse Native crystal structure of mltf pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P11
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane-bound lytic murein transglycosylase F
- EC
- 4.2.2.-
- UniProt
- Q9HXN1
- Ligands
- MG, CL
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane-bound lytic murein transglycosylase F (EC 4.2.2.-) | protein | 428 | 50% helix, 14% strand | Q9HXN1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.70 | 0.87 | 42 | empty |
| 2 | 380 | 0.57 | 0.75 | 38 | CL |
| 3 | 99 | 0.45 | 0.79 | 23 | empty |
| 4 | 134 | 0.43 | 0.75 | 22 | empty |
| 5 | 125 | 0.38 | 0.74 | 20 | empty |
Compared structures
- 4P11 · Native crystal structure of MltF Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HXN1 · AlphaFold monomer V2.0 prediction for membrane-bound lytic murein transglycosylase F… · a predicted model of the same protein · 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 Q9HXN1
- Elsewhere: RCSB PDB 4P11 · PDBe 4P11 · UniProt Q9HXN1
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