Research workbench
Crystal structure of mycolic acid cyclopropane synthase CMAA1 complexed with sah and ctab
Analyse Crystal structure of mycolic acid cyclopropane synthase CMAA1 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KPG
- Type
- protein
- Length
- 1,137 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclopropane-fatty-acyl-phospholipid synthase 1
- EC
- 2.1.1.79
- UniProt
- Q11195
- Ligands
- SAH, 16A, CO3
- Pockets
- 11 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Cyclopropane-fatty-acyl-phospholipid synthase 1 (EC 2.1.1.79) | protein | 285 | 47% helix, 16% strand | Q11195 |
| B | Cyclopropane-fatty-acyl-phospholipid synthase 1 (EC 2.1.1.79) | protein | 284 | 49% helix, 17% strand | Q11195 |
| D | Cyclopropane-fatty-acyl-phospholipid synthase 1 (EC 2.1.1.79) | protein | 283 | 49% helix, 16% strand | Q11195 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 4 copies · chains A, B, C, D
- 16A · Cetyl-trimethyl-ammonium · ligand · 4 copies · chains A, B, C, D
- CO3 · Carbonate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 417 | 0.86 | 0.93 | 64 | CO3, SAH, 16A |
| 2 | 378 | 0.86 | 0.94 | 58 | CO3, SAH, 16A |
| 3 | 1060 | 0.81 | 0.83 | 100 | empty |
| 4 | 166 | 0.81 | 0.97 | 35 | SAH |
| 5 | 163 | 0.80 | 0.96 | 33 | SAH |
Interfaces
6 interfaces between chains.
- A–C · 684 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 352 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 199 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 104 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 16 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 modified (engineered).
Compared structures
- 1KPG · Crystal Structure of mycolic acid cyclopropane synthase CmaA1 complexed with SAH and CTAB · 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 Q11195
- Elsewhere: RCSB PDB 1KPG · PDBe 1KPG · UniProt Q11195
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