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The crystal structure of the human IRP60 ectodomain
Analyse The crystal structure of the human IRP60 ectodomain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q87
- Type
- protein
- Length
- 320 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CMRF35-H antigen
- UniProt
- Q9UGN4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CMRF35-H antigen | protein | 107 | 8% helix, 47% strand | Q9UGN4 |
| B | CMRF35-H antigen | protein | 107 | 8% helix, 48% strand | Q9UGN4 |
| C | CMRF35-H antigen | protein | 106 | 11% helix, 46% strand | Q9UGN4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 572 | 0.66 | 0.76 | 52 | empty |
| 2 | 57 | 0.29 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 605 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 570 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 54 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 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 Q9UGN4
- Elsewhere: RCSB PDB 2Q87 · PDBe 2Q87 · UniProt Q9UGN4
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