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Specificity and structure of a high affinity activin-like 1 (ALK1) signaling complex
Analyse Specificity and structure of a high affinity activin-like 1 (ALK1) signaling… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FAO
- Type
- protein
- Length
- 3,233 residues
- Chains
- 36
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GROWTH/DIFFERENTIATION factor 2; SERINE/THREONINE-protein kinase receptor R3; Activin…
- UniProt
- Q9UK05, P37023, Q13705
- Ligands
- NAG, NA
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 5 distinct chains · 11% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, G, H, M, S, T, a, b, g, h | GROWTH/DIFFERENTIATION factor 2 | protein | 105 | 14% helix, 50% strand | Q9UK05 |
| C, I, O, U, c, i | SERINE/THREONINE-protein kinase receptor R3 | protein | 75 | 7% helix, 35% strand | P37023 |
| D, J, P, V, d, j | SERINE/THREONINE-protein kinase receptor R3 | protein | 72 | 7% helix, 36% strand | P37023 |
| E, F, K, L, Q, R, W, X, e, f, k, l | Activin receptor type-2B | protein | 91 | 8% helix, 48% strand | Q13705 |
| N | GROWTH/DIFFERENTIATION factor 2 | protein | 104 | 18% helix, 48% strand | Q9UK05 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 24 copies · chains E, F, K, L, Q, R, W, l, X, k, e, f
- NA · Sodium ion · metal · 6 copies · chains F, G, K, R, T, X, a, e, k
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 734 | 0.79 | 0.83 | 73 | empty |
| 2 | 795 | 0.73 | 0.79 | 71 | empty |
| 3 | 810 | 0.73 | 0.78 | 66 | empty |
| 4 | 476 | 0.72 | 0.82 | 49 | empty |
| 5 | 195 | 0.72 | 0.89 | 32 | empty |
Interfaces
69 interfaces between chains.
- g–h · 1305 Ų buried · 7 hydrogen bonds · protein-protein
- a–b · 1304 Ų buried · 7 hydrogen bonds · protein-protein
- S–T · 1300 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 1299 Ų buried · 7 hydrogen bonds · protein-protein
- M–N · 1299 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 162 disulfide, 24 glycan (disulfide, N-glycosylation).
Compared structures
- 4FAO · Specificity and Structure of a high affinity Activin-like 1 (ALK1) signaling complex · the same entry in another collection · chain K against K, 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
- Every structure of UniProt Q9UK05
- Every structure of UniProt P37023
- Every structure of UniProt Q13705
- Elsewhere: RCSB PDB 4FAO · PDBe 4FAO · UniProt Q9UK05 · UniProt P37023 · UniProt Q13705
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