Research workbench
Cmci-N160 sah
Analyse Cmci-N160 sah in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BR5
- Type
- protein
- Length
- 1,315 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cephalosporin hydroxylase cmci
- UniProt
- O85726
- Ligands
- SAH
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 6 distinct chains · 31% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cephalosporin hydroxylase cmci | protein | 226 | 32% helix, 17% strand | O85726 |
| B | Cephalosporin hydroxylase cmci | protein | 232 | 32% helix, 18% strand | O85726 |
| C | Cephalosporin hydroxylase cmci | protein | 227 | 33% helix, 18% strand | O85726 |
| D | Cephalosporin hydroxylase cmci | protein | 194 | 27% helix, 20% strand | O85726 |
| E | Cephalosporin hydroxylase cmci | protein | 230 | 30% helix, 17% strand | O85726 |
| F | Cephalosporin hydroxylase cmci | protein | 206 | 29% helix, 19% strand | O85726 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.76 | 0.97 | 20 | empty |
| 2 | 1190 | 0.76 | 0.78 | 95 | SAH |
| 3 | 70 | 0.75 | 0.99 | 23 | empty |
| 4 | 80 | 0.75 | 0.97 | 21 | empty |
| 5 | 1042 | 0.73 | 0.77 | 93 | SAH |
Interfaces
6 interfaces between chains.
- A–B · 2699 Ų buried · 47 hydrogen bonds · protein-protein
- C–F · 2674 Ų buried · 45 hydrogen bonds · protein-protein
- D–E · 2559 Ų buried · 44 hydrogen bonds · protein-protein
- A–E · 1758 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1753 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 2BR5 · cmcI-N160 SAH · the same entry in another collection · chain A against A, 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 O85726
- Elsewhere: RCSB PDB 2BR5 · PDBe 2BR5 · UniProt O85726
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