Research workbench

Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted 4-vinyl-1-cyclohexene 1,2-epoxide hydrolysis intermediate

Analyse Crystal structure of the E153Q mutant of the cftr inhibitory factor cif… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TNJ
Type: protein
Length: 1,174 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cftr inhibitory factor
UniProt: A0A0M3KL26
Ligands: BVH, DVH, AVH, 8MD
Pockets: 8 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Cftr inhibitory factor	protein	294	42% helix, 20% strand	A0A0M3KL26
B, C	Cftr inhibitory factor	protein	293	43% helix, 20% strand	A0A0M3KL26

Ligands and binding sites

BVH · (1R,2R,4S)-4-ethenylcyclohexane-1,2-diol · ligand · 3 copies · chains B, C, D
DVH · (1S,2S,4R)-4-ethenylcyclohexane-1,2-diol · ligand · 3 copies · chains B, C, D
AVH · (1R,2R,4R)-4-ethenylcyclohexane-1,2-diol · ligand · chains A
8MD · (1S,2S,4S)-4-ethenylcyclohexane-1,2-diol · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	282	0.79	0.91	42	empty
2	478	0.77	0.85	65	empty
3	284	0.62	0.80	31	empty
4	256	0.62	0.81	31	empty
5	162	0.56	0.82	24	empty

Interfaces

5 interfaces between chains.

A–B · 1426 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 1410 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 608 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 604 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 420 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 covalent, 4 disulfide (covalent ligand, disulfide).

Compared structures

5TNJ · Crystal structure of the E153Q mutant of the CFTR inhibitory factor Cif containing the… · 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 A0A0M3KL26
Elsewhere: RCSB PDB 5TNJ · PDBe 5TNJ · UniProt A0A0M3KL26

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