Research workbench
Crystal structure of conserved protein of unknown function from enterococcus faecalis V583 at 2.4 a resolution, probable N- acyltransferase
Analyse Crystal structure of conserved protein of unknown function from enterococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HV2
- Type
- protein
- Length
- 2,349 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- Q836T6
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 5 distinct chains · 33% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 392 | 32% helix, 33% strand | Q836T6 |
| B | Hypothetical protein | protein | 393 | 33% helix, 34% strand | Q836T6 |
| C, E | Hypothetical protein | protein | 391 | 33% helix, 33% strand | Q836T6 |
| D | Hypothetical protein | protein | 390 | 33% helix, 34% strand | Q836T6 |
| F | Hypothetical protein | protein | 392 | 32% helix, 33% strand | Q836T6 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 6 copies · chains A, B, C, D, E, F
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 5 copies · chains A, C, B, F, E, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 655 | 0.80 | 0.85 | 103 | EPE |
| 2 | 1018 | 0.78 | 0.80 | 79 | empty |
| 3 | 556 | 0.78 | 0.84 | 72 | empty |
| 4 | 519 | 0.77 | 0.84 | 74 | empty |
| 5 | 1014 | 0.76 | 0.78 | 106 | EPE |
Interfaces
12 interfaces between chains.
- C–D · 1582 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 1554 Ų buried · 24 hydrogen bonds · protein-protein
- E–F · 1519 Ų buried · 25 hydrogen bonds · protein-protein
- C–E · 560 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 553 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 70 modified (engineered).
Compared structures
- 2HV2 · Crystal Structure of Conserved Protein of Unknown Function from Enterococcus faecalis… · 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 Q836T6
- Elsewhere: RCSB PDB 2HV2 · PDBe 2HV2 · UniProt Q836T6
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