MolNFT v1 · #178046 · protein

Fmnb complexed with ADP

7F2U · FAD:PROTEIN FMN transferase: “Fmnb complexed with ADP”. X-ray diffraction, 2 ligands (ADP, MG), 7 pockets (best druggability 0.79). MolNFT v1 #178046 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7F2U
Type: protein
Length: 643 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD:PROTEIN FMN transferase
EC: 2.7.1.180
UniProt: A0A0H3GJF7
Ligands: ADP, MG
Pockets: 7 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD:PROTEIN FMN transferase (EC 2.7.1.180)	protein	322	32% helix, 27% strand	A0A0H3GJF7
B	FAD:PROTEIN FMN transferase (EC 2.7.1.180)	protein	321	32% helix, 29% strand	A0A0H3GJF7

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	526	0.79	0.86	51	ADP, MG
2	463	0.79	0.87	47	ADP, MG
3	439	0.61	0.76	47	empty
4	166	0.51	0.79	36	empty
5	138	0.47	0.78	27	empty

Interfaces

1 interface between chains.

A–B · 328 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

7F2U · FmnB complexed with ADP · 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 A0A0H3GJF7
Elsewhere: RCSB PDB 7F2U · PDBe 7F2U · UniProt A0A0H3GJF7

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