MolNFT v1 · #111075 · protein

X-ray structure of the 4-N-formyltransferase viof from providencia alcalifaciens O30

4YFV: “X-ray structure of the 4-N-formyltransferase viof from providencia alcalifaciens O30”. X-ray diffraction, 1 ligand (CL), 4 pockets (best druggability 0.68). MolNFT v1 #111075 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4YFV
Type: protein
Length: 482 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Viof
UniProt: M9P0Q2
Ligands: CL
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Viof	protein	244	35% helix, 27% strand	M9P0Q2
B	Viof	protein	238	36% helix, 28% strand	M9P0Q2

Ligands and binding sites

CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	470	0.68	0.79	45	empty
2	537	0.66	0.76	43	empty
3	105	0.42	0.77	23	EDO
4	100	0.38	0.76	24	EDO

Interfaces

1 interface between chains.

A–B · 1580 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

4YFV · X-ray structure of the 4-N-formyltransferase VioF from Providencia alcalifaciens O30 · 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 M9P0Q2
Elsewhere: RCSB PDB 4YFV · PDBe 4YFV · UniProt M9P0Q2

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