MolNFT v1 · #86511 · protein

Ferrichrome-bound FHUD2

4B8Y: “Ferrichrome-bound FHUD2”. X-ray diffraction, 3 ligands (AHO, FE, CL), 3 pockets (best druggability 0.53). MolNFT v1 #86511 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4B8Y
Type: protein
Length: 280 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FHUD2; Virulence factor
UniProt: Q2FVW9
Ligands: AHO, FE, CL
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FHUD2	protein	277	45% helix, 21% strand	Q2FVW9
B	Virulence factor	protein	3	0% helix, 0% strand	—

Ligands and binding sites

AHO · N-acetyl-N-hydroxy-L-ornithine · ligand · 3 copies · chains A, B
FE · Fe (III) ion · metal · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 10 copies · 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	208	0.53	0.77	29	AHO, EDO, FE
2	64	0.31	0.75	16	EDO
3	61	0.30	0.75	16	EDO

Interfaces

1 interface between chains.

A–B · 122 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

4B8Y · Ferrichrome-bound FhuD2 · 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 Q2FVW9
Elsewhere: RCSB PDB 4B8Y · PDBe 4B8Y · UniProt Q2FVW9

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