Research workbench
Carbamate kinase from enterococcus faecalis bound to a sulfate ion and two water molecules, which mimic the substrate carbamyl phosphate
Analyse Carbamate kinase from enterococcus faecalis bound to a sulfate ion and two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WE4
- Type
- protein
- Length
- 1,236 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbamate kinase 1
- EC
- 2.7.2.2
- UniProt
- P0A2X7
- Ligands
- SO4
- Pockets
- 18 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Carbamate kinase 1 (EC 2.7.2.2) | protein | 309 | 39% helix, 24% strand | P0A2X7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 15 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.62 | 0.74 | 53 | SO4 |
| 2 | 352 | 0.60 | 0.77 | 48 | SO4 |
| 3 | 380 | 0.60 | 0.76 | 49 | SO4 |
| 4 | 383 | 0.59 | 0.76 | 55 | SO4 |
| 5 | 323 | 0.57 | 0.76 | 48 | SO4 |
Interfaces
4 interfaces between chains.
- B–D · 2099 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 2086 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 109 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 84 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2WE4 · Carbamate kinase from Enterococcus faecalis bound to a sulfate ion and two water… · the same entry in another collection · chain D against D, TM-score 1.00
- P0A2X7 · AlphaFold monomer V2.0 prediction for carbamate kinase 1 (P0A2X7) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P0A2X7
- Elsewhere: RCSB PDB 2WE4 · PDBe 2WE4 · UniProt P0A2X7
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