MolNFT v1 · #187316 · protein

Structure of the core postfusion porcine endogenous retrovirus fusion protein

7S94 · Endogenous retrovirus group S71 member 1 env polyprotein: “Structure of the core postfusion porcine endogenous retrovirus fusion protein”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.36). MolNFT v1 #187316 on…

PDB: 7S94
Type: protein
Length: 527 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endogenous retrovirus group S71 member 1 env polyprotein
UniProt: B3VQ66
Ligands: CL
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 6 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endogenous retrovirus group S71 member 1 env polyprotein	protein	92	83% helix, 0% strand	B3VQ66
B	Endogenous retrovirus group S71 member 1 env polyprotein	protein	89	81% helix, 0% strand	B3VQ66
C	Endogenous retrovirus group S71 member 1 env polyprotein	protein	97	82% helix, 0% strand	B3VQ66
D	Endogenous retrovirus group S71 member 1 env polyprotein	protein	90	83% helix, 0% strand	B3VQ66
E	Endogenous retrovirus group S71 member 1 env polyprotein	protein	76	76% helix, 0% strand	B3VQ66
F	Endogenous retrovirus group S71 member 1 env polyprotein	protein	83	82% helix, 0% strand	B3VQ66

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B, C, D, E, F
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B, E

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.36	0.76	21	empty
2	66	0.33	0.75	14	empty

Interfaces

6 interfaces between chains.

A–C · 1587 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1572 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1540 Å² buried · 19 hydrogen bonds · protein-protein
D–F · 1421 Å² buried · 18 hydrogen bonds · protein-protein
E–F · 1355 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

7S94 · Structure of the core postfusion porcine endogenous retrovirus fusion protein · 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 B3VQ66
Elsewhere: RCSB PDB 7S94 · PDBe 7S94 · UniProt B3VQ66

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