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Structure of CBIO1 from clostridium perfringens: part of the ABC transporter complex cbionq.

Analyse Structure of CBIO1 from clostridium perfringens: part of the ABC transporter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GFO
Type: protein
Length: 251 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cobalt import ATP-binding protein cbio 1
EC: 3.6.3.-
UniProt: Q0TUN8
Ligands: SO4
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cobalt import ATP-binding protein cbio 1 (EC 3.6.3.-)	protein	251	43% helix, 25% strand	Q0TUN8

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.46	0.75	21	empty
2	96	0.39	0.76	19	empty

Compared structures

3GFO · Structure of cbiO1 from clostridium perfringens: Part of the ABC transporter complex… · the same entry in another collection · chain A against A, TM-score 1.00
Q0TUN8 · AlphaFold monomer V2.0 prediction for energy-coupling factor transporter ATP-binding… · a predicted model of the same protein · chain A against A, TM-score 0.87

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 Q0TUN8
Elsewhere: RCSB PDB 3GFO · PDBe 3GFO · UniProt Q0TUN8

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