MolNFT v1 · #146585 · protein

Ftsy-ng domain bound to fragment 3.

6DLX · Signal recognition particle receptor ftsy: “Ftsy-ng domain bound to fragment 3.”. X-ray diffraction, 2 ligands (GXY, NH4), 3 pockets (best druggability 0.80). MolNFT v1 #146585 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6DLX
Type: protein
Length: 600 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Signal recognition particle receptor ftsy
UniProt: A0A1M2TDP9
Ligands: GXY, NH4
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Signal recognition particle receptor ftsy	protein	300	53% helix, 13% strand	A0A1M2TDP9

Ligands and binding sites

GXY · 4-bromo-2,5-dimethoxyaniline · ligand · 4 copies · chains A, B
NH4 · Ammonium ion · ion · 17 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	824	0.80	0.83	67	PEG
2	95	0.41	0.77	25	GXY, NH4
3	66	0.35	0.77	21	GXY

Interfaces

1 interface between chains.

A–B · 667 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6DLX · FtsY-NG domain bound to fragment 3. · 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 A0A1M2TDP9
Elsewhere: RCSB PDB 6DLX · PDBe 6DLX · UniProt A0A1M2TDP9

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