Research workbench
Cryo-EM structure of the E. COLI CTP synthase tetramer
Analyse Cryo-EM structure of the E. COLI CTP synthase tetramer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U05
- Type
- protein
- Length
- 2,136 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CTP synthase
- EC
- 6.3.4.2
- UniProt
- B7MLA1
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | CTP synthase (EC 6.3.4.2) | protein | 534 | 41% helix, 22% strand | B7MLA1 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 826 | 0.82 | 0.84 | 101 | empty |
| 2 | 769 | 0.82 | 0.84 | 86 | empty |
| 3 | 428 | 0.76 | 0.85 | 53 | empty |
| 4 | 386 | 0.75 | 0.86 | 52 | empty |
| 5 | 494 | 0.74 | 0.83 | 74 | empty |
Interfaces
6 interfaces between chains.
- A–B · 791 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 779 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 544 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 542 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 300 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 B7MLA1
- Elsewhere: RCSB PDB 5U05 · PDBe 5U05 · UniProt B7MLA1
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