Research workbench
Crystal structure of human chondroadherin
Analyse Crystal structure of human chondroadherin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LFN
- Type
- protein
- Length
- 1,296 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chondroadherin
- UniProt
- O15335
- Ligands
- CL
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chondroadherin | protein | 324 | 8% helix, 17% strand | O15335 |
| C | Chondroadherin | protein | 323 | 8% helix, 18% strand | O15335 |
| D | Chondroadherin | protein | 325 | 8% helix, 17% strand | O15335 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1192 | 0.82 | 0.83 | 113 | empty |
| 2 | 978 | 0.81 | 0.82 | 97 | empty |
| 3 | 148 | 0.51 | 0.80 | 24 | empty |
| 4 | 138 | 0.43 | 0.76 | 28 | empty |
| 5 | 57 | 0.38 | 0.80 | 15 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1069 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 870 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 453 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 134 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 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 O15335
- Elsewhere: RCSB PDB 5LFN · PDBe 5LFN · UniProt O15335
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