Research workbench

S. solfataricus ABCE1 post-splitting state

Analyse S. solfataricus ABCE1 post-splitting state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LW7
Type: protein
Length: 593 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 17.0
Source: Pyrococcus abyssi (strain GE5 / Orsay)
Molecule: ABC transporter ATP-binding protein
UniProt: Q9UZA4
Ligands: SF4
Pockets: 7 · best druggability 0.62

Structure

electron microscopy · resolution 17.0 · 1 distinct chain · 32% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	ABC transporter ATP-binding protein	protein	593	32% helix, 19% strand	Q9UZA4

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · 2 copies · chains 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	374	0.62	0.78	48	empty
2	283	0.54	0.76	34	empty
3	117	0.42	0.76	21	empty
4	102	0.39	0.75	16	empty
5	68	0.38	0.79	18	empty

Modifications

Observed in the structure: 2 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

5LW7 · S. solfataricus ABCE1 post-splitting state · the same entry in another collection · chain B against B, 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 Q9UZA4
Elsewhere: RCSB PDB 5LW7 · PDBe 5LW7 · UniProt Q9UZA4

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