Research workbench
Crystal structure of C163, a backbone circularized G-csf
Analyse Crystal structure of C163, a backbone circularized G-csf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GW9
- Type
- protein
- Length
- 652 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Granulocyte colony-stimulating factor
- UniProt
- P09919
- Pockets
- 7 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Granulocyte colony-stimulating factor | protein | 163 | 69% helix, 0% strand | P09919 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 503 | 0.65 | 0.77 | 55 | empty |
| 2 | 447 | 0.63 | 0.77 | 60 | empty |
| 3 | 160 | 0.54 | 0.80 | 25 | empty |
| 4 | 143 | 0.53 | 0.81 | 31 | empty |
| 5 | 117 | 0.38 | 0.74 | 23 | empty |
Interfaces
4 interfaces between chains.
- A–C · 1060 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 699 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 463 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 166 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 5GW9 · Crystal structure of C163, a backbone circularized G-CSF · the same entry in another collection · chain D against D, TM-score 1.00
- P09919 · AlphaFold monomer V2.0 prediction for granulocyte colony-stimulating factor (P09919) · a predicted model of the same protein · chain D against A, TM-score 0.91
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 P09919
- Elsewhere: RCSB PDB 5GW9 · PDBe 5GW9 · UniProt P09919
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