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Ftp from Treponema pallidum bound to an ADP-like inhibitor

Analyse Ftp from Treponema pallidum bound to an ADP-like inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MGT
Type: protein
Length: 319 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.54
Source: Treponema pallidum
Molecule: FAD:protein FMN transferase
EC: 2.7.1.180
UniProt: A0A5J6YQV1
Ligands: ZD4, MG
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · resolution 1.54 · 1 distinct chain · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD:protein FMN transferase (EC 2.7.1.180)	protein	319	33% helix, 29% strand	A0A5J6YQV1

Ligands and binding sites

ZD4 · 2-chloroadenosine 5'-(trihydrogen diphosphate) · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

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	501	0.73	0.82	53	MG, ZD4, EDO
2	63	0.35	0.77	17	empty
3	59	0.29	0.75	16	empty

Compared structures

7MGT · Ftp from treponema pallidum bound to an ADP-like inhibitor · 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 A0A5J6YQV1
Elsewhere: RCSB PDB 7MGT · PDBe 7MGT · UniProt A0A5J6YQV1

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