MolNFT v1 · #174365 · protein
Mevo lectin complex with alpha-mannose
7BT9: “Mevo lectin complex with alpha-mannose”. X-ray diffraction, 1 ligand (MAN), 20 pockets (best druggability 0.67). MolNFT v1 #174365 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7BT9
- Type
- protein
- Length
- 1,948 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lectin
- UniProt
- D7DTD6
- Ligands
- MAN
- Pockets
- 20 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, D, E, F, C, H, J, K, L, M, N | Lectin | protein | 140 | 0% helix, 61% strand | D7DTD6 |
| G, I | Lectin | protein | 134 | 0% helix, 61% strand | D7DTD6 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 14 copies · chains B, G, A, D, E, F, C, H, I, J, K, L, M, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 435 | 0.67 | 0.80 | 57 | empty |
| 2 | 501 | 0.60 | 0.74 | 67 | MAN |
| 3 | 386 | 0.57 | 0.75 | 37 | empty |
| 4 | 240 | 0.51 | 0.76 | 26 | empty |
| 5 | 186 | 0.46 | 0.75 | 38 | empty |
Interfaces
24 interfaces between chains.
- B–E · 671 Ų buried · 20 hydrogen bonds · protein-protein
- H–L · 665 Ų buried · 19 hydrogen bonds · protein-protein
- M–N · 661 Ų buried · 15 hydrogen bonds · protein-protein
- J–K · 657 Ų buried · 17 hydrogen bonds · protein-protein
- F–C · 657 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7BT9 · Mevo lectin complex with alpha-mannose · 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 D7DTD6
- Elsewhere: RCSB PDB 7BT9 · PDBe 7BT9 · UniProt D7DTD6
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