MolNFT v1 · #1471 · protein
Barnase wildtype structure at pH 7.5 from a CRYO_COOLED crystal at 100K
1B2X · Protein (barnase): “Barnase wildtype structure at pH 7.5 from a CRYO_COOLED crystal at 100K”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.66). MolNFT v1 #1471 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1B2X
- Type
- protein
- Length
- 324 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (barnase)
- EC
- 3.1.27.3
- UniProt
- P00648
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Protein (barnase) (EC 3.1.27.3) | protein | 108 | 23% helix, 23% strand | P00648 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 532 | 0.66 | 0.77 | 55 | empty |
| 2 | 66 | 0.30 | 0.74 | 20 | empty |
Interfaces
3 interfaces between chains.
- B–C · 222 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 166 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 38 Ų buried · 0 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 P00648
- Elsewhere: RCSB PDB 1B2X · PDBe 1B2X · UniProt P00648
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