MolNFT v1 · #139925 · protein
Complex structure (RMMAN134A-M6).
5XUL · Endo-1,4-beta-mannanase: “Complex structure (RMMAN134A-M6).”. X-ray diffraction, 1 ligand (BMA), 4 pockets (best druggability 0.55). MolNFT v1 #139925 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5XUL
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-mannanase
- UniProt
- A0A0A1NDE2
- Ligands
- BMA
- Pockets
- 4 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Endo-1,4-beta-mannanase | protein | 159 | 62% helix, 9% strand | A0A0A1NDE2 |
Ligands and binding sites
- BMA · beta-D-mannopyranose · sugar · 12 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.55 | 0.78 | 39 | empty |
| 2 | 150 | 0.51 | 0.79 | 20 | empty |
| 3 | 110 | 0.40 | 0.76 | 20 | BMA |
| 4 | 93 | 0.37 | 0.75 | 21 | BMA |
Interfaces
1 interface between chains.
- B–A · 661 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5XUL · Complex structure (RmMan134A-M6). · the same entry in another collection · chain B against B, 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 A0A0A1NDE2
- Elsewhere: RCSB PDB 5XUL · PDBe 5XUL · UniProt A0A0A1NDE2
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