MolNFT v1 · #135062 · protein

Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted (R)-1,2-epoxyoctane hydrolysis intermediate

5TNM: “Crystal structure of the E153Q mutant of the cftr inhibitory factor cif containing the adducted…”. X-ray diffraction, 1 ligand (7F2), 8 pockets (best druggability 0.81). MolNFT v1 #135062 on GenesisL1: 3D structure, binding sites…

PDB: 5TNM
Type: protein
Length: 1,181 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cftr inhibitory factor
UniProt: A0A0M3KL26
Ligands: 7F2
Pockets: 8 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Cftr inhibitory factor	protein	296	42% helix, 20% strand	A0A0M3KL26
C	Cftr inhibitory factor	protein	293	44% helix, 20% strand	A0A0M3KL26

Ligands and binding sites

7F2 · (2R)-octane-1,2-diol · ligand · 4 copies · chains A, B, C, D

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

Pockets

8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	869	0.81	0.84	99	7F2
2	289	0.79	0.91	41	empty
3	55	0.71	0.98	19	7F2
4	312	0.63	0.79	33	empty
5	148	0.61	0.84	35	7F2

Interfaces

5 interfaces between chains.

A–B · 1424 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 1416 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 607 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 601 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 465 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

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

Compared structures

5TNM · 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 5TNM · PDBe 5TNM · UniProt A0A0M3KL26

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