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Crystal structure of a single-chain trimer of human adiponectin globular domain

Analyse Crystal structure of a single-chain trimer of human adiponectin globular domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DOU
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adiponectin
UniProt: Q15848
Ligands: CA, NA
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adiponectin	protein	399	0% helix, 59% strand	Q15848

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
NA · Sodium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	382	0.76	0.86	23	EDO
2	63	0.35	0.77	13	empty

Compared structures

4DOU · Crystal Structure of a Single-chain Trimer of Human Adiponectin Globular Domain · the same entry in another collection · chain A against A, TM-score 1.00
Q15848 · AlphaFold monomer V2.0 prediction for adiponectin (Q15848) · a predicted model of the same protein · chain A against A, TM-score 0.34

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 Q15848
Elsewhere: RCSB PDB 4DOU · PDBe 4DOU · UniProt Q15848

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