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Crystal structure of sterol carrier protein 2

Analyse Crystal structure of sterol carrier protein 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CX7
Type: protein
Length: 259 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sterol carrier protein 2
UniProt: Q5SL92
Ligands: PO4
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sterol carrier protein 2	protein	129	42% helix, 28% strand	Q5SL92
B	Sterol carrier protein 2	protein	130	45% helix, 28% strand	Q5SL92

Ligands and binding sites

PO4 · Phosphate ion · ion · chains B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.80	0.98	25	empty
2	139	0.71	0.90	31	empty
3	110	0.40	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 427 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified, 2 disulfide (engineered, disulfide).

Compared structures

2CX7 · Crystal structure of sterol carrier protein 2 · 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 Q5SL92
Elsewhere: RCSB PDB 2CX7 · PDBe 2CX7 · UniProt Q5SL92

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