Research workbench
Structure of menh from S. aureus
Analyse Structure of menh from S. aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XMZ
- Type
- protein
- Length
- 266 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrolase, ALPHA/BETA hydrolase fold family
- EC
- 4.2.99.20
- UniProt
- Q5HH39
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydrolase, ALPHA/BETA hydrolase fold family (EC 4.2.99.20) | protein | 266 | 50% helix, 15% strand | Q5HH39 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.71 | 0.84 | 52 | empty |
Compared structures
- 2XMZ · Structure of MenH from S. aureus · the same entry in another collection · 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 Q5HH39
- Elsewhere: RCSB PDB 2XMZ · PDBe 2XMZ · UniProt Q5HH39
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