Research workbench
Crystal structure of BH2602 protein from bacillus halodurans with CoA, northeast structural genomics consortium target BHR199
Analyse Crystal structure of BH2602 protein from bacillus halodurans with CoA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NWZ
- Type
- protein
- Length
- 599 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BH2602 protein
- UniProt
- Q9K9P3
- Ligands
- COA, SO4
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BH2602 protein | protein | 155 | 27% helix, 34% strand | Q9K9P3 |
| B | BH2602 protein | protein | 151 | 30% helix, 34% strand | Q9K9P3 |
| C | BH2602 protein | protein | 151 | 30% helix, 31% strand | Q9K9P3 |
| D | BH2602 protein | protein | 142 | 27% helix, 35% strand | Q9K9P3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 439 | 0.79 | 0.87 | 61 | empty |
| 2 | 554 | 0.76 | 0.82 | 62 | SO4 |
| 3 | 573 | 0.73 | 0.81 | 53 | COA |
| 4 | 460 | 0.69 | 0.80 | 46 | empty |
| 5 | 67 | 0.41 | 0.80 | 21 | empty |
Interfaces
6 interfaces between chains.
- A–C · 2029 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 1894 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 696 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 649 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 393 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 23 modified (engineered).
Compared structures
- 3NWZ · Crystal Structure of BH2602 protein from Bacillus halodurans with CoA, Northeast… · 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 Q9K9P3
- Elsewhere: RCSB PDB 3NWZ · PDBe 3NWZ · UniProt Q9K9P3
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