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Crystal structure of human syncytin 2 in post-fusion conformation

Analyse Crystal structure of human syncytin 2 in post-fusion conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RX3
Type: protein
Length: 274 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Syncytin-2
UniProt: P60508
Ligands: CL

Structure

x-ray diffraction · 3 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Syncytin-2	protein	89	83% helix, 0% strand	P60508
B	Syncytin-2	protein	86	77% helix, 0% strand	P60508
C	Syncytin-2	protein	99	84% helix, 0% strand	P60508

Ligands and binding sites

CL · Chloride ion · ion · chains A, B, C

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

Interfaces

3 interfaces between chains.

B–C · 1581 Å² buried · 20 hydrogen bonds · protein-protein
A–C · 1577 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 1523 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6RX3 · Crystal structure of human syncytin 2 in post-fusion conformation · the same entry in another collection · chain B against B, TM-score 1.00
P60508 · AlphaFold monomer V2.0 prediction for syncytin-2 (P60508) · a predicted model of the same protein · chain B against A, TM-score 0.83

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 P60508
Elsewhere: RCSB PDB 6RX3 · PDBe 6RX3 · UniProt P60508

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