MolNFT v1 · #152045 · protein

Cryo-EM informed directed evolution of nitrilase 4 leads to a change in quaternary structure.

6I5T · Bifunctional NITRILASE/NITRILE hydratase NIT4: “Cryo-EM informed directed evolution of nitrilase 4 leads to a change in quaternary structure.”. Electron microscopy, 17 pockets (best druggability 0.79). MolNFT v1 #152045 on…

PDB: 6I5T
Type: protein
Length: 1,734 residues
Chains: 6
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: 17 · best druggability 0.79

Structure

electron microscopy · 1 distinct chain · 20% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F, E, D, C, B, A	Bifunctional NITRILASE/NITRILE hydratase NIT4 (EC 3.5.5.1, 3.5.5.4, 4.2.1.65)	protein	289	20% helix, 20% strand	P46011

Pockets

17 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	849	0.79	0.82	93	empty
2	813	0.78	0.81	97	empty
3	138	0.60	0.84	21	empty
4	135	0.59	0.84	21	empty
5	99	0.59	0.87	22	empty

Interfaces

11 interfaces between chains.

F–E · 2047 Å² buried · 25 hydrogen bonds · protein-protein
D–C · 2042 Å² buried · 25 hydrogen bonds · protein-protein
B–A · 2039 Å² buried · 25 hydrogen bonds · protein-protein
D–B · 1206 Å² buried · 15 hydrogen bonds · protein-protein
C–A · 1206 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6I5T · Cryo-EM informed directed evolution of Nitrilase 4 leads to a change in quaternary… · the same entry in another collection · chain D against D, TM-score 1.00
P46011 · AlphaFold monomer V2.0 prediction for bifunctional NITRILASE/NITRILE hydratase NIT4… · a predicted model of the same protein · chain F against A, TM-score 0.96

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 6I5T · PDBe 6I5T · UniProt P46011

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.