Research workbench
Structure analysis of (POG)4-log-(POG)5
Analyse Structure analysis of (POG)4-log-(POG)5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DRT
- Type
- protein
- Length
- 86 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen like peptide
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Collagen like peptide | protein | 29 | 0% helix, 0% strand | — |
| C | Collagen like peptide | protein | 28 | 0% helix, 0% strand | — |
Ligands and binding sites
- EOH · Ethanol · additive · 3 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- B–C · 909 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 891 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 872 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 29 modified (hydroxylation).
Compared structures
- 2DRT · Structure Analysis of (POG)4-LOG-(POG)5 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 2DRT · PDBe 2DRT
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