Research workbench
Crystal structure of the starter condensation domain of rhizomide synthetase rzma
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
- 7C1H
- Type
- protein
- Length
- 1,603 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-ribosomal peptide synthetase modules
- EC
- 6.3.2.-
- UniProt
- E5ATN9
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-ribosomal peptide synthetase modules (EC 6.3.2.-) | protein | 410 | 37% helix, 25% strand | E5ATN9 |
| B | Non-ribosomal peptide synthetase modules (EC 6.3.2.-) | protein | 391 | 37% helix, 25% strand | E5ATN9 |
| C | Non-ribosomal peptide synthetase modules (EC 6.3.2.-) | protein | 408 | 37% helix, 26% strand | E5ATN9 |
| D | Non-ribosomal peptide synthetase modules (EC 6.3.2.-) | protein | 394 | 39% helix, 24% strand | E5ATN9 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1019 | 0.85 | 0.86 | 102 | empty |
| 2 | 955 | 0.85 | 0.86 | 102 | empty |
| 3 | 1162 | 0.83 | 0.84 | 105 | empty |
| 4 | 886 | 0.83 | 0.85 | 76 | empty |
| 5 | 597 | 0.76 | 0.83 | 65 | empty |
Interfaces
4 interfaces between chains.
- B–C · 579 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 533 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 496 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 13 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7C1H · Crystal structure of the starter condensation domain of rhizomide synthetase RzmA · 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 7C1H · PDBe 7C1H · UniProt E5ATN9
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