MolNFT v1 · #31796 · protein
X-ray crystal structure of protein HI1161 from haemophilus influenzae. northeast structural genomics consortium target IR63.
2B6E · Hypothetical UPF0152 protein HI1161: “X-ray crystal structure of protein HI1161 from haemophilus influenzae. northeast structural genomics…”. X-ray diffraction, 11 pockets (best druggability 0.78). MolNFT v1 #31796 on GenesisL1: 3D…
- PDB
- 2B6E
- Type
- protein
- Length
- 1,111 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical UPF0152 protein HI1161
- UniProt
- P45083
- Pockets
- 11 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 22% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, H | Hypothetical UPF0152 protein HI1161 | protein | 137 | 22% helix, 41% strand | P45083 |
| B, C | Hypothetical UPF0152 protein HI1161 | protein | 139 | 21% helix, 42% strand | P45083 |
| D | Hypothetical UPF0152 protein HI1161 | protein | 146 | 25% helix, 40% strand | P45083 |
| F, G | Hypothetical UPF0152 protein HI1161 | protein | 138 | 21% helix, 42% strand | P45083 |
Ligands and binding sites
- ACY · Acetic acid · additive · 8 copies · chains B, C, A, D, E, G, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 970 | 0.78 | 0.80 | 106 | empty |
| 2 | 342 | 0.69 | 0.82 | 47 | empty |
| 3 | 375 | 0.68 | 0.80 | 45 | empty |
| 4 | 305 | 0.67 | 0.82 | 46 | empty |
| 5 | 310 | 0.67 | 0.81 | 46 | empty |
Interfaces
13 interfaces between chains.
- G–H · 1260 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1237 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1216 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 1200 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 544 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2B6E · X-Ray Crystal Structure of Protein HI1161 from Haemophilus influenzae. Northeast… · the same entry in another collection · chain H against H, TM-score 1.00
- P45083 · AlphaFold monomer V2.0 prediction for putative esterase HI_1161 (P45083) · 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 P45083
- Elsewhere: RCSB PDB 2B6E · PDBe 2B6E · UniProt P45083
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