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Crystal structure of CFL1 wild-type from burkholderia cenocepacia

Analyse Crystal structure of CFL1 wild-type from burkholderia cenocepacia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7JQX
Type: protein
Length: 1,176 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cif-like 1 wild-type
UniProt: B4EJL9
Pockets: 9 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cif-like 1 wild-type	protein	294	46% helix, 18% strand	B4EJL9

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	303	0.68	0.83	36	empty
2	180	0.68	0.86	30	empty
3	286	0.67	0.83	36	empty
4	170	0.66	0.86	32	empty
5	168	0.66	0.86	31	empty

Interfaces

3 interfaces between chains.

B–C · 545 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 459 Å² buried · 4 hydrogen bonds · protein-protein
B–D · 455 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7JQX · Crystal structure of Cfl1 wild-type from Burkholderia cenocepacia · 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 B4EJL9
Elsewhere: RCSB PDB 7JQX · PDBe 7JQX · UniProt B4EJL9

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