Research workbench
Crystal structure the N-terminal domain of E. COLI hisb. apo mg model.
Analyse Crystal structure the N-terminal domain of E. COLI hisb. apo mg model. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FPR
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine biosynthesis bifunctional protein hisb
- EC
- 3.1.3.15
- UniProt
- Q9S5G5
- Ligands
- ZN, MG, NA, BR
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine biosynthesis bifunctional protein hisb (EC 3.1.3.15) | protein | 156 | 38% helix, 22% strand | Q9S5G5 |
| B | Histidine biosynthesis bifunctional protein hisb (EC 3.1.3.15) | protein | 160 | 38% helix, 21% strand | Q9S5G5 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- NA · Sodium ion · metal · chains B
- BR · Bromide ion · ion · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.50 | 0.82 | 17 | MG, BR |
| 2 | 80 | 0.48 | 0.83 | 17 | NA, BR |
Interfaces
1 interface between chains.
- A–B · 634 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2FPR · Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model. · the same entry in another collection · chain A against A, TM-score 1.00
- Q9S5G5 · AlphaFold monomer V2.0 prediction for histidine biosynthesis bifunctional protein hisb… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9S5G5
- Elsewhere: RCSB PDB 2FPR · PDBe 2FPR · UniProt Q9S5G5
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