Research workbench
Structure of human CXCR1 in phospholipid bilayers
Analyse Structure of human CXCR1 in phospholipid bilayers in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LNL
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-X-C chemokine receptor type 1
- UniProt
- P25024
- Pockets
- 5 · best druggability 0.81
Structure
solid-state nmr · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-X-C chemokine receptor type 1 | protein | 296 | 71% helix, 0% strand | P25024 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.81 | 0.94 | 34 | empty |
| 2 | 77 | 0.73 | 0.97 | 22 | empty |
| 3 | 137 | 0.68 | 0.88 | 23 | empty |
| 4 | 115 | 0.43 | 0.77 | 19 | empty |
| 5 | 82 | 0.34 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 P25024
- Elsewhere: RCSB PDB 2LNL · PDBe 2LNL · UniProt P25024
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