Research workbench
Structure of GP41 T21/CP621-652
Analyse Structure of GP41 T21/CP621-652 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VGX
- Type
- protein
- Length
- 66 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope glycoprotein GP160
- UniProt
- P03375
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 2 distinct chains · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Envelope glycoprotein GP160 | protein | 38 | 95% helix, 0% strand | P03375 |
| D | Envelope glycoprotein GP160 | protein | 28 | 82% helix, 0% strand | P03375 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains C
- NH2 · Amino group · ion · chains C
- ACY · Acetic acid · additive · chains C
- GOL · Glycerol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- C–D · 443 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 3VGX · Structure of gp41 T21/Cp621-652 · the same entry in another collection · chain C against C, 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 P03375
- Elsewhere: RCSB PDB 3VGX · PDBe 3VGX · UniProt P03375
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