Research workbench
Structure of 6-aminohexanoate-oligomer hydrolase
Analyse Structure of 6-aminohexanoate-oligomer hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AXG
- Type
- protein
- Length
- 5,158 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endotype 6-aminohexanoat-oligomer hydrolase
- UniProt
- Q1EPR5
- Ligands
- NA
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, L, M, N, O | Endotype 6-aminohexanoat-oligomer hydrolase | protein | 344 | 25% helix, 31% strand | Q1EPR5 |
| K | Endotype 6-aminohexanoat-oligomer hydrolase | protein | 342 | 24% helix, 31% strand | Q1EPR5 |
Ligands and binding sites
- NA · Sodium ion · metal · 6 copies · chains A, K, L, M, N, O
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 | 88 | 0.77 | 0.98 | 22 | empty |
| 2 | 1072 | 0.76 | 0.78 | 124 | empty |
| 3 | 80 | 0.76 | 0.98 | 22 | empty |
| 4 | 86 | 0.75 | 0.98 | 22 | empty |
| 5 | 82 | 0.75 | 0.98 | 21 | empty |
Interfaces
22 interfaces between chains.
- E–G · 3260 Ų buried · 47 hydrogen bonds · protein-protein
- A–B · 3248 Ų buried · 46 hydrogen bonds · protein-protein
- J–L · 3237 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 3213 Ų buried · 47 hydrogen bonds · protein-protein
- I–K · 3207 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 3AXG · Structure of 6-aminohexanoate-oligomer hydrolase · the same entry in another collection · chain O against O, 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 Q1EPR5
- Elsewhere: RCSB PDB 3AXG · PDBe 3AXG · UniProt Q1EPR5
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