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Crystal structure of human fibroblast activation protein alpha
Analyse Crystal structure of human fibroblast activation protein alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z68
- Type
- protein
- Length
- 1,438 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast activation protein, alpha subunit
- EC
- 3.4.21.-
- UniProt
- Q12884
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fibroblast activation protein, alpha subunit (EC 3.4.21.-) | protein | 719 | 18% helix, 35% strand | Q12884 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.73 | 0.98 | 26 | empty |
| 2 | 330 | 0.67 | 0.81 | 58 | empty |
| 3 | 394 | 0.67 | 0.80 | 62 | empty |
| 4 | 308 | 0.59 | 0.77 | 44 | empty |
| 5 | 331 | 0.59 | 0.77 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 2137 Ų buried · 31 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 glycan, 8 disulfide (N-glycosylation, 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 Q12884
- Elsewhere: RCSB PDB 1Z68 · PDBe 1Z68 · UniProt Q12884
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