MolNFT v1 · #151853 · protein
Cryo-EM informed directed evolution of nitrilase 4 leads to a change in quaternary structure.
6I00 · Bifunctional NITRILASE/NITRILE hydratase NIT4: “Cryo-EM informed directed evolution of nitrilase 4 leads to a change in quaternary structure.”. Electron microscopy, 20 pockets (best druggability 0.77). MolNFT v1 #151853 on…
- PDB
- 6I00
- Type
- protein
- Length
- 3,468 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional NITRILASE/NITRILE hydratase NIT4
- EC
- 3.5.5.1, 3.5.5.4, 4.2.1.65
- UniProt
- P46011
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 18% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| J, I, H, G, F, E, D, C, B, A, L, K | Bifunctional NITRILASE/NITRILE hydratase NIT4 (EC 3.5.5.1, 3.5.5.4, 4.2.1.65) | protein | 289 | 18% helix, 25% strand | P46011 |
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 | 731 | 0.77 | 0.82 | 86 | empty |
| 2 | 697 | 0.77 | 0.82 | 83 | empty |
| 3 | 768 | 0.77 | 0.81 | 90 | empty |
| 4 | 750 | 0.77 | 0.81 | 93 | empty |
| 5 | 695 | 0.76 | 0.81 | 85 | empty |
Interfaces
27 interfaces between chains.
- F–E · 2015 Ų buried · 32 hydrogen bonds · protein-protein
- L–K · 2014 Ų buried · 31 hydrogen bonds · protein-protein
- B–A · 2008 Ų buried · 31 hydrogen bonds · protein-protein
- H–G · 2008 Ų buried · 32 hydrogen bonds · protein-protein
- J–I · 2003 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 6I00 · Cryo-EM informed directed evolution of Nitrilase 4 leads to a change in quaternary… · the same entry in another collection · chain K against K, 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 P46011
- Elsewhere: RCSB PDB 6I00 · PDBe 6I00 · UniProt P46011
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