MolNFT v1 · #89339 · protein

Crystal structure of the cftr inhibitory factor cif with the E153Q mutation

4DMC · Putative hydrolase: “Crystal structure of the cftr inhibitory factor cif with the E153Q mutation”. X-ray diffraction, 9 pockets (best druggability 0.81). MolNFT v1 #89339 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4DMC
Type: protein
Length: 1,184 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative hydrolase
UniProt: Q02P97
Pockets: 9 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Putative hydrolase	protein	296	43% helix, 18% strand	Q02P97

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	326	0.81	0.91	47	empty
2	315	0.80	0.91	50	empty
3	53	0.70	0.97	19	empty
4	243	0.62	0.81	27	empty
5	252	0.62	0.80	29	empty

Interfaces

5 interfaces between chains.

A–B · 1422 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 1408 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 647 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 633 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 474 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4DMC · Crystal structure of the CFTR inhibitory factor Cif with the E153Q mutation · 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 Q02P97
Elsewhere: RCSB PDB 4DMC · PDBe 4DMC · UniProt Q02P97

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