Research workbench
Crystal structure of uncharacterized protein EAH89906
Analyse Crystal structure of uncharacterized protein EAH89906 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FEQ
- Type
- protein
- Length
- 6,471 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative amidohydrolase
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 7 distinct chains · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F, G, H, I, P | Putative amidohydrolase | protein | 405 | 33% helix, 24% strand | — |
| C, M | Putative amidohydrolase | protein | 406 | 33% helix, 24% strand | — |
| J | Putative amidohydrolase | protein | 402 | 34% helix, 25% strand | — |
| K | Putative amidohydrolase | protein | 403 | 36% helix, 25% strand | — |
| L | Putative amidohydrolase | protein | 404 | 37% helix, 25% strand | — |
| N | Putative amidohydrolase | protein | 404 | 34% helix, 25% strand | — |
| O | Putative amidohydrolase | protein | 401 | 34% helix, 25% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 32 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1064 | 0.83 | 0.84 | 99 | empty |
| 2 | 507 | 0.81 | 0.88 | 76 | empty |
| 3 | 649 | 0.81 | 0.85 | 78 | empty |
| 4 | 543 | 0.81 | 0.87 | 65 | empty |
| 5 | 416 | 0.81 | 0.89 | 54 | empty |
Interfaces
36 interfaces between chains.
- L–M · 768 Ų buried · 16 hydrogen bonds · protein-protein
- L–O · 759 Ų buried · 1 hydrogen bond · protein-protein
- K–P · 758 Ų buried · 1 hydrogen bond · protein-protein
- I–J · 757 Ų buried · 1 hydrogen bond · protein-protein
- M–N · 752 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 3FEQ · PDBe 3FEQ
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