Research workbench
Human platelet profilin complexed with an L-PRO10- iodotyrosine peptide
Analyse Human platelet profilin complexed with an L-PRO10- iodotyrosine peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CF0
- Type
- protein
- Length
- 285 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (profilin); Protein (L-PRO10-iodotyrosine)
- UniProt
- P07737
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (profilin) | protein | 138 | 28% helix, 32% strand | P07737 |
| C | Protein (L-PRO10-iodotyrosine) | protein | 9 | 0% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.40 | 0.74 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–C · 421 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 348 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 97 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
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 P07737
- Elsewhere: RCSB PDB 1CF0 · PDBe 1CF0 · UniProt P07737
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