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Crystal structure of human squamous cell carcinoma antigen 1
Analyse Crystal structure of human squamous cell carcinoma antigen 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZV6
- Type
- protein
- Length
- 1,071 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serpin B3
- UniProt
- P29508
- Pockets
- 17 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serpin B3 | protein | 350 | 31% helix, 29% strand | P29508 |
| B | Serpin B3 | protein | 371 | 29% helix, 25% strand | P29508 |
| C | Serpin B3 | protein | 350 | 33% helix, 27% strand | P29508 |
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.70 | 0.78 | 74 | empty |
| 2 | 108 | 0.57 | 0.84 | 25 | empty |
| 3 | 111 | 0.56 | 0.84 | 21 | empty |
| 4 | 100 | 0.56 | 0.85 | 25 | empty |
| 5 | 121 | 0.52 | 0.81 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–C · 428 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 370 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 243 Ų buried · 4 hydrogen bonds · protein-protein
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 P29508
- Elsewhere: RCSB PDB 2ZV6 · PDBe 2ZV6 · UniProt P29508
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