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Crystal structure of mycobacterial ftsx extracellular domain

Analyse Crystal structure of mycobacterial ftsx extracellular domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N8N
Type: protein
Length: 403 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsx
UniProt: P9WG19
Ligands: K
Pockets: 5 · best druggability 0.55

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsx	protein	102	42% helix, 23% strand	P9WG19
B	Cell division protein ftsx	protein	103	42% helix, 21% strand	P9WG19
C, D	Cell division protein ftsx	protein	99	44% helix, 22% strand	P9WG19

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains B, C, A, D

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	311	0.55	0.75	38	empty
2	66	0.51	0.86	21	empty
3	51	0.42	0.83	19	empty
4	123	0.39	0.74	21	empty
5	98	0.36	0.75	18	empty

Interfaces

3 interfaces between chains.

A–B · 550 Å² buried · 1 hydrogen bond · protein-protein
B–C · 497 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 495 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4N8N · Crystal structure of Mycobacterial FtsX extracellular domain · the same entry in another collection · chain D against D, TM-score 1.00
P9WG19 · AlphaFold monomer V2.0 prediction for cell division protein ftsx (P9WG19) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P9WG19
Elsewhere: RCSB PDB 4N8N · PDBe 4N8N · UniProt P9WG19

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