Research workbench
HIV-1 ca 1/2-hexamer-ee
Analyse HIV-1 ca 1/2-hexamer-ee in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ECN
- Type
- protein
- Length
- 1,101 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 ca
- UniProt
- P04591, A0A248SME6
- Pockets
- 15 · best druggability 0.72
Structure
x-ray diffraction · 6 distinct chains · 61% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIV-1 ca | protein | 201 | 62% helix, 2% strand | P04591 |
| B | HIV-1 ca | protein | 207 | 61% helix, 2% strand | P04591 |
| C | HIV-1 ca | protein | 145 | 58% helix, 4% strand | A0A248SME6 |
| D | HIV-1 ca | protein | 207 | 60% helix, 3% strand | P04591 |
| E | HIV-1 ca | protein | 199 | 63% helix, 1% strand | P04591 |
| F | HIV-1 ca | protein | 142 | 59% helix, 6% strand | A0A248SME6 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.72 | 0.76 | 87 | empty |
| 2 | 72 | 0.70 | 0.95 | 18 | empty |
| 3 | 894 | 0.70 | 0.75 | 115 | empty |
| 4 | 528 | 0.62 | 0.75 | 70 | empty |
| 5 | 465 | 0.59 | 0.74 | 56 | empty |
Interfaces
5 interfaces between chains.
- D–F · 1144 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1130 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 1112 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1070 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 835 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 6ECN · HIV-1 CA 1/2-hexamer-EE · 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 P04591
- Every structure of UniProt A0A248SME6
- Elsewhere: RCSB PDB 6ECN · PDBe 6ECN · UniProt P04591 · UniProt A0A248SME6
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