Research workbench
Crystal structure of chicken MHC class II for 1.9 ångström
Analyse Crystal structure of chicken MHC class II for 1.9 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KVM
- Type
- protein
- Length
- 380 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MHC class II alpha chain; MHC class II beta chain 2; Peptide from 60S ribosomal protein…
- UniProt
- Q4U5Z6, Q4U600, P67883
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MHC class II alpha chain | protein | 184 | 16% helix, 46% strand | Q4U5Z6 |
| B | MHC class II beta chain 2 | protein | 179 | 20% helix, 46% strand | Q4U600 |
| C | Peptide from 60S ribosomal protein L30 | protein | 17 | 0% helix, 6% strand | P67883 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.56 | 0.81 | 30 | empty |
| 2 | 85 | 0.38 | 0.76 | 19 | empty |
| 3 | 80 | 0.32 | 0.74 | 19 | empty |
| 4 | 73 | 0.31 | 0.74 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2707 Ų buried · 45 hydrogen bonds · protein-protein
- B–C · 713 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 673 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 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 Q4U5Z6
- Every structure of UniProt Q4U600
- Every structure of UniProt P67883
- Elsewhere: RCSB PDB 6KVM · PDBe 6KVM · UniProt Q4U5Z6 · UniProt Q4U600 · UniProt P67883
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