Research workbench
Crystal structure of the D1607N mutant form of thioesterase domain of mtb PKS13
Analyse Crystal structure of the D1607N mutant form of thioesterase domain of mtb PKS13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V3Z
- Type
- protein
- Length
- 550 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyketide synthase PKS13 (termination polyketide synthase)
- EC
- 2.7.7.-
- UniProt
- A0A0T9CRX1
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyketide synthase PKS13 (termination polyketide synthase) (EC 2.7.7.-) | protein | 276 | 46% helix, 17% strand | A0A0T9CRX1 |
| B | Polyketide synthase PKS13 (termination polyketide synthase) (EC 2.7.7.-) | protein | 274 | 45% helix, 17% strand | A0A0T9CRX1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 766 | 0.74 | 0.79 | 78 | 1PE |
| 2 | 686 | 0.70 | 0.77 | 53 | 1PE |
| 3 | 325 | 0.56 | 0.75 | 35 | empty |
| 4 | 61 | 0.41 | 0.80 | 15 | empty |
| 5 | 90 | 0.35 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 577 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5V3Z · Crystal Structure of the D1607N mutant form of Thioesterase domain of Mtb Pks13 · 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 A0A0T9CRX1
- Elsewhere: RCSB PDB 5V3Z · PDBe 5V3Z · UniProt A0A0T9CRX1
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