Research workbench
Solution structure of the human chemokine hcc-2, NMR, 30 structures
Analyse Solution structure of the human chemokine hcc-2, NMR, 30 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HCC
- Type
- protein
- Length
- 66 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human chemokine hcc-2
- UniProt
- Q16663
Structure
solution nmr · 1 distinct chain · 15% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human chemokine hcc-2 | protein | 66 | 15% helix, 24% strand | Q16663 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2HCC · Solution structure of the human chemokine hcc-2, NMR, 30 structures · the same entry in another collection · chain A against A, TM-score 1.00
- Q16663 · AlphaFold monomer V2.0 prediction for C-C motif chemokine 15 (Q16663) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 Q16663
- Elsewhere: RCSB PDB 2HCC · PDBe 2HCC · UniProt Q16663
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