MolNFT v1 · #111988 · protein

Soluble binding domain of LMO1422 ABC-transporter

4Z7E · LMO1422 protein: “Soluble binding domain of LMO1422 ABC-transporter”. X-ray diffraction, 5 pockets (best druggability 0.49). MolNFT v1 #111988 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4Z7E
Type: protein
Length: 540 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LMO1422 protein
UniProt: Q8Y775
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	LMO1422 protein	protein	270	49% helix, 18% strand	Q8Y775

Ligands and binding sites

PPI · Propanoic acid · additive · 4 copies · chains A, B
1PE · Pentaethylene glycol · additive · 2 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B

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

Pockets

5 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	200	0.49	0.76	30	PPI
2	202	0.48	0.75	30	PPI
3	161	0.44	0.75	24	empty
4	133	0.43	0.76	19	empty
5	141	0.37	0.72	24	empty

Interfaces

1 interface between chains.

A–B · 63 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4Z7E · Soluble binding domain of Lmo1422 ABC-transporter · 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 Q8Y775
Elsewhere: RCSB PDB 4Z7E · PDBe 4Z7E · UniProt Q8Y775

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