Research workbench
Crystal structure of fmta from staphylococcus aureus at 2.58 a
Analyse Crystal structure of fmta from staphylococcus aureus at 2.58 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZH8
- Type
- protein
- Length
- 707 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein fmta
- UniProt
- O50608
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein fmta | protein | 358 | 36% helix, 19% strand | O50608 |
| B | Protein fmta | protein | 349 | 36% helix, 19% strand | O50608 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
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 | 568 | 0.67 | 0.77 | 66 | empty |
| 2 | 260 | 0.62 | 0.80 | 45 | empty |
| 3 | 133 | 0.43 | 0.75 | 23 | empty |
| 4 | 90 | 0.36 | 0.75 | 23 | empty |
| 5 | 65 | 0.35 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 870 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5ZH8 · Crystal Structure of FmtA from Staphylococcus aureus at 2.58 A · the same entry in another collection · chain A against A, TM-score 1.00
- O50608 · AlphaFold monomer V2.0 prediction for teichoic acid D-alanine hydrolase (O50608) · a predicted model of the same protein · chain B 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 O50608
- Elsewhere: RCSB PDB 5ZH8 · PDBe 5ZH8 · UniProt O50608
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