MolNFT v1 · #104170 · protein
Bovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5B
4Q2K · Chymotrypsinogen a: “Bovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5B”. X-ray diffraction, 1 ligand (5BF), 6 pockets (best druggability 0.76). MolNFT v1 #104170 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4Q2K
- Type
- protein
- Length
- 928 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chymotrypsinogen a
- EC
- 3.4.21.1
- UniProt
- P00766
- Ligands
- 5BF
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 12% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chymotrypsinogen a (EC 3.4.21.1) | protein | 231 | 12% helix, 35% strand | P00766 |
| B | Chymotrypsinogen a (EC 3.4.21.1) | protein | 231 | 11% helix, 36% strand | P00766 |
| C | Chymotrypsinogen a (EC 3.4.21.1) | protein | 234 | 12% helix, 33% strand | P00766 |
| D | Chymotrypsinogen a (EC 3.4.21.1) | protein | 232 | 12% helix, 36% strand | P00766 |
Ligands and binding sites
- 5BF · (11S)-4,9-dioxo-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-17,22-dioxa-10,30-diazatetracyclo[21.2.2.2~13,16~.1~5,8~]triaconta-1(25),5,7,13,15,23,26,28-octaene-11-carboxamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 883 | 0.76 | 0.80 | 96 | 5BF |
| 2 | 855 | 0.74 | 0.78 | 85 | 5BF |
| 3 | 234 | 0.53 | 0.77 | 43 | empty |
| 4 | 181 | 0.48 | 0.76 | 36 | 5BF |
| 5 | 157 | 0.43 | 0.75 | 27 | empty |
Interfaces
4 interfaces between chains.
- A–B · 436 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 369 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 364 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 302 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide, 4 covalent (disulfide, covalent ligand).
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 P00766
- Elsewhere: RCSB PDB 4Q2K · PDBe 4Q2K · UniProt P00766
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.