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Contribution of a buried hydrogen bond to HIV-1 envelope glycoprotein structure and function

Analyse Contribution of a buried hydrogen bond to HIV-1 envelope glycoprotein structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F23
Type: protein
Length: 440 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transmembrane glycoprotein
UniProt: Q89797

Structure

x-ray diffraction · 5 distinct chains · 87% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transmembrane glycoprotein	protein	74	85% helix, 0% strand	Q89797
B	Transmembrane glycoprotein	protein	72	86% helix, 0% strand	Q89797
C	Transmembrane glycoprotein	protein	71	87% helix, 0% strand	Q89797
D, E	Transmembrane glycoprotein	protein	75	91% helix, 0% strand	Q89797
F	Transmembrane glycoprotein	protein	73	88% helix, 0% strand	Q89797

Interfaces

6 interfaces between chains.

D–E · 1319 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 1257 Å² buried · 8 hydrogen bonds · protein-protein
D–F · 1232 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 1208 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 1186 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1F23 · Contribution of a buried hydrogen bond to HIV-1 envelope glycoprotein structure and… · 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 Q89797
Elsewhere: RCSB PDB 1F23 · PDBe 1F23 · UniProt Q89797

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