MolNFT v1 · #164304 · protein
Crystal structure of the cc-chemokine 5 (CCL5) E66S mutation
6STK · C-C motif chemokine 5: “Crystal structure of the cc-chemokine 5 (CCL5) E66S mutation”. X-ray diffraction. MolNFT v1 #164304 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6STK
- Type
- protein
- Length
- 129 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-C motif chemokine 5
- UniProt
- P13501
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-C motif chemokine 5 | protein | 65 | 20% helix, 31% strand | P13501 |
| B | C-C motif chemokine 5 | protein | 64 | 20% helix, 30% strand | P13501 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 800 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 P13501
- Elsewhere: RCSB PDB 6STK · PDBe 6STK · UniProt P13501
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