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ATP-binding domain of haemolysin B from escherichia COLI

Analyse ATP-binding domain of haemolysin B from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MT0
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Haemolysin secretion ATP-binding protein
UniProt: P08716
Ligands: SO4
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Haemolysin secretion ATP-binding protein	protein	241	34% helix, 25% strand	P08716

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	147	0.44	0.76	22	empty
2	114	0.42	0.76	18	empty

Compared structures

1MT0 · ATP-binding domain of hemolysin B from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
P08716 · AlphaFold monomer V2.0 prediction for alpha-hemolysin translocation ATP-binding protein… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P08716
Elsewhere: RCSB PDB 1MT0 · PDBe 1MT0 · UniProt P08716

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