Research workbench

Escherichia COLI ytfe E159L

Analyse Escherichia COLI ytfe E159L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BHB
Type: protein
Length: 435 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iron-sulfur cluster repair protein ytfe
UniProt: W8TAR7
Ligands: FE
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 67% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Iron-sulfur cluster repair protein ytfe	protein	216	69% helix, 1% strand	W8TAR7
B	Iron-sulfur cluster repair protein ytfe	protein	219	65% helix, 1% strand	W8TAR7

Ligands and binding sites

FE · Fe (III) ion · metal · 2 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	524	0.60	0.74	51	empty
2	139	0.56	0.83	19	empty
3	175	0.54	0.79	23	empty
4	165	0.46	0.76	25	empty

Interfaces

1 interface between chains.

A–B · 150 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7BHB · Escherichia coli YtfE E159L · 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 W8TAR7
Elsewhere: RCSB PDB 7BHB · PDBe 7BHB · UniProt W8TAR7

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