MolNFT v1 · #148638 · protein
Crystal structure of an endo-laminarinase from formosa HEL1_33_131
6FCG · Glycoside hydrolase, GH17 family: “Crystal structure of an endo-laminarinase from formosa HEL1_33_131”. X-ray diffraction, 1 ligand (CA), 18 pockets (best druggability 0.80). MolNFT v1 #148638 on GenesisL1: 3D structure, binding…
- PDB
- 6FCG
- Type
- protein
- Length
- 2,358 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase, GH17 family
- UniProt
- A0A1D7Y259
- Ligands
- CA
- Pockets
- 18 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Glycoside hydrolase, GH17 family | protein | 393 | 41% helix, 15% strand | A0A1D7Y259 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B, E, A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 845 | 0.80 | 0.82 | 92 | empty |
| 2 | 1037 | 0.79 | 0.81 | 92 | empty |
| 3 | 788 | 0.79 | 0.82 | 89 | empty |
| 4 | 800 | 0.79 | 0.82 | 84 | empty |
| 5 | 617 | 0.71 | 0.79 | 60 | empty |
Interfaces
9 interfaces between chains.
- C–D · 1007 Ų buried · 15 hydrogen bonds · protein-protein
- B–F · 986 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 971 Ų buried · 13 hydrogen bonds · protein-protein
- B–E · 961 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 961 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6FCG · Crystal structure of an endo-laminarinase from Formosa Hel1_33_131 · 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 A0A1D7Y259
- Elsewhere: RCSB PDB 6FCG · PDBe 6FCG · UniProt A0A1D7Y259
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