MolNFT v1 · #151181 · protein

Crystal structure of extracellular domain 1 (ECD1) of ftsx from S. pneumonie in complex with N-decyl-B-D-maltoside

6HFX · Cell division protein ftsx: “Crystal structure of extracellular domain 1 (ECD1) of ftsx from S. pneumonie in complex with…”. X-ray diffraction, 2 pockets (best druggability 0.37). MolNFT v1 #151181 on GenesisL1: 3D structure…

PDB: 6HFX
Type: protein
Length: 228 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsx
UniProt: A0A0I6INF5
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Cell division protein ftsx	protein	114	31% helix, 28% strand	A0A0I6INF5

Ligands and binding sites

DMU · Decyl-beta-D-maltopyranoside · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.37	0.75	14	empty
2	52	0.25	0.73	14	empty

Interfaces

1 interface between chains.

B–A · 195 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6HFX · Crystal structure of Extracellular Domain 1 (ECD1) of FtsX from S. pneumonie in complex… · the same entry in another collection · chain B against B, 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 A0A0I6INF5
Elsewhere: RCSB PDB 6HFX · PDBe 6HFX · UniProt A0A0I6INF5

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