MolNFT v1 · #115539 · protein
Artificial HIV fusion inhibitor AP1 fused to the C-terminus of GP41 nhr
5CMU · Envelope GLYCOPROTEIN,AP1: “Artificial HIV fusion inhibitor AP1 fused to the C-terminus of GP41 nhr”. X-ray diffraction. MolNFT v1 #115539 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5CMU
- Type
- protein
- Length
- 217 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope GLYCOPROTEIN,AP1
- UniProt
- Q1HMR5
Structure
x-ray diffraction · 2 distinct chains · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Envelope GLYCOPROTEIN,AP1 | protein | 73 | 82% helix, 0% strand | Q1HMR5 |
| B, C | Envelope GLYCOPROTEIN,AP1 | protein | 72 | 89% helix, 0% strand | Q1HMR5 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1339 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1311 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 1277 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5CMU · Artificial HIV fusion inhibitor AP1 fused to the C-terminus of gp41 NHR · 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 Q1HMR5
- Elsewhere: RCSB PDB 5CMU · PDBe 5CMU · UniProt Q1HMR5
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