Research workbench
Crystal structure of masl, a thiolase from massilia sp. YMA4
Analyse Crystal structure of masl, a thiolase from massilia sp. YMA4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EI3
- Type
- protein
- Length
- 1,572 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA C-acyltransferase
- EC
- 2.3.1.16
- UniProt
- A0A5C7BKK5
- Pockets
- 14 · best druggability 0.61
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA C-acyltransferase (EC 2.3.1.16) | protein | 392 | 39% helix, 24% strand | A0A5C7BKK5 |
| B, C | Acetyl-CoA C-acyltransferase (EC 2.3.1.16) | protein | 393 | 39% helix, 24% strand | A0A5C7BKK5 |
| D | Acetyl-CoA C-acyltransferase (EC 2.3.1.16) | protein | 394 | 39% helix, 24% strand | A0A5C7BKK5 |
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.61 | 0.81 | 41 | empty |
| 2 | 192 | 0.60 | 0.82 | 38 | empty |
| 3 | 176 | 0.60 | 0.82 | 37 | empty |
| 4 | 187 | 0.59 | 0.81 | 37 | empty |
| 5 | 101 | 0.45 | 0.79 | 23 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2619 Ų buried · 61 hydrogen bonds · protein-protein
- A–B · 2611 Ų buried · 61 hydrogen bonds · protein-protein
- A–C · 816 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 800 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 394 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7EI3 · Crystal structure of MasL, a thiolase from Massilia sp. YMA4 · 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 A0A5C7BKK5
- Elsewhere: RCSB PDB 7EI3 · PDBe 7EI3 · UniProt A0A5C7BKK5
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