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Crystal structure of Apo Caenorhabditis elegans lipid binding protein 8 (LBP-8)

Analyse Crystal structure of Apo Caenorhabditis elegans lipid binding protein 8 (LBP-8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6C1Z
Type: protein
Length: 138 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.3
Source: Caenorhabditis elegans
Molecule: Lipid Binding Protein
UniProt: O02324
Ligands: SO4
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · resolution 1.3 · 1 distinct chain · 15% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipid Binding Protein	protein	138	15% helix, 54% strand	O02324

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	359	0.82	0.91	44	empty

Compared structures

6C1Z · Crystal structure of apo caenorhabditis elegans lipid binding protein 8 (lbp-8) · the same entry in another collection · chain A against A, TM-score 1.00
O02324 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein homolog 8 (O02324) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O02324
Elsewhere: RCSB PDB 6C1Z · PDBe 6C1Z · UniProt O02324

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