Research workbench
Crystal structure of the starter condensation domain of rhizomide synthetase RzmA mutant R148A
Analyse Crystal structure of the starter condensation domain of rhizomide synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C1K
- Type
- protein
- Length
- 1,614 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.755
- Source
- Paraburkholderia rhizoxinica HKI 454
- Molecule
- Non-ribosomal peptide synthetase modules
- EC
- 6.3.2.-
- UniProt
- E5ATN9
- Pockets
- 16 · best druggability 0.84
Structure
x-ray diffraction · resolution 2.755 · 3 distinct chains · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Non-ribosomal peptide synthetase modules (EC 6.3.2.-) | protein | 409 | 35% helix, 25% strand | E5ATN9 |
| B | Non-ribosomal peptide synthetase modules (EC 6.3.2.-) | protein | 397 | 39% helix, 22% strand | E5ATN9 |
| D | Non-ribosomal peptide synthetase modules (EC 6.3.2.-) | protein | 399 | 38% helix, 23% strand | E5ATN9 |
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1068 | 0.84 | 0.85 | 109 | empty |
| 2 | 1128 | 0.84 | 0.85 | 121 | empty |
| 3 | 918 | 0.84 | 0.85 | 98 | empty |
| 4 | 1158 | 0.82 | 0.83 | 107 | empty |
| 5 | 382 | 0.74 | 0.85 | 53 | empty |
Interfaces
4 interfaces between chains.
- A–D · 603 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 475 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 423 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 24 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7C1K · Crystal structure of the starter condensation domain of rhizomide synthetase rzma mutant… · 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 E5ATN9
- Elsewhere: RCSB PDB 7C1K · PDBe 7C1K · UniProt E5ATN9
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