Research workbench
Crystal structure of se-met mltf from pseudomonas aeruginosa
Analyse Crystal structure of se-met mltf from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A5X
- Type
- protein
- Length
- 837 residues
- Chains
- 2
- 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
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane-bound lytic murein transglycosylase F (EC 4.2.2.-) | protein | 420 | 48% helix, 16% strand | Q9HXN1 |
| B | Membrane-bound lytic murein transglycosylase F (EC 4.2.2.-) | protein | 417 | 49% helix, 16% strand | Q9HXN1 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 489 | 0.79 | 0.87 | 51 | EDO |
| 2 | 582 | 0.78 | 0.84 | 49 | EDO |
| 3 | 735 | 0.74 | 0.79 | 103 | EDO |
| 4 | 173 | 0.66 | 0.86 | 39 | empty |
| 5 | 200 | 0.58 | 0.80 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 889 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 5A5X · Crystal Structure of Se-Met MltF from Pseudomonas aeruginosa · the same entry in another collection · chain B against B, 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 0.65
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 5A5X · PDBe 5A5X · UniProt Q9HXN1
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