Research workbench

Crystal structure of leporine serum albumin

Analyse Crystal structure of leporine serum albumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F5V
Type: protein
Length: 584 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serum albumin
UniProt: G1U9S2
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serum albumin	protein	584	71% helix, 0% strand	G1U9S2

Ligands and binding sites

PGE · Triethylene glycol · additive · 2 copies · chains A
ACT · Acetate ion · additive · 2 copies · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	798	0.77	0.81	82	PG4, ACT
2	855	0.77	0.80	65	empty
3	137	0.75	0.93	26	empty
4	114	0.70	0.91	21	PGE
5	240	0.59	0.79	25	empty

Modifications

Observed in the structure: 17 disulfide (disulfide).

Compared structures

4F5V · Crystal Structure of Leporine Serum Albumin · 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 G1U9S2
Elsewhere: RCSB PDB 4F5V · PDBe 4F5V · UniProt G1U9S2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.