MolNFT v1 · #167803 · protein
Anti-tryptase Fab E104.V1 bound to tryptase
6VVU: “Anti-tryptase Fab E104.V1 bound to tryptase”. X-ray diffraction, 1 ligand (CA). MolNFT v1 #167803 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VVU
- Type
- protein
- Length
- 2,706 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15661
- Ligands
- CA
Structure
x-ray diffraction · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 244 | — | Q15661 |
| B | — | protein | 245 | — | Q15661 |
| D, C | — | protein | 243 | — | Q15661 |
| E, H | — | protein | 216 | — | — |
| F, I | — | protein | 216 | — | — |
| G | — | protein | 217 | — | — |
| J | — | protein | 219 | — | — |
| K | — | protein | 216 | — | — |
| L | — | protein | 215 | — | — |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VVU · Anti-Tryptase fab E104.v1 bound to tryptase · the same entry in another collection · chain L against L, 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 Q15661
- Elsewhere: RCSB PDB 6VVU · PDBe 6VVU · UniProt Q15661
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