Research workbench
Crystal structure of carbon-sulfur lyase involved in aluminum resistance (YP_878183.1) from clostridium novyi nt at 2.90 a resolution
Analyse Crystal structure of carbon-sulfur lyase involved in aluminum resistance… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GWP
- Type
- protein
- Length
- 1,696 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon-sulfur lyase involved in aluminum resistance
- UniProt
- A0Q0N1
- Pockets
- 15 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon-sulfur lyase involved in aluminum resistance | protein | 424 | 43% helix, 14% strand | A0Q0N1 |
| B, D | Carbon-sulfur lyase involved in aluminum resistance | protein | 427 | 44% helix, 13% strand | A0Q0N1 |
| C | Carbon-sulfur lyase involved in aluminum resistance | protein | 418 | 44% helix, 13% strand | A0Q0N1 |
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 637 | 0.86 | 0.91 | 66 | empty |
| 2 | 1008 | 0.81 | 0.83 | 143 | empty |
| 3 | 505 | 0.70 | 0.80 | 38 | empty |
| 4 | 581 | 0.70 | 0.79 | 71 | empty |
| 5 | 526 | 0.68 | 0.78 | 38 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2602 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 2559 Ų buried · 23 hydrogen bonds · protein-protein
- B–D · 2307 Ų buried · 29 hydrogen bonds · protein-protein
- A–C · 2175 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 241 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 47 modified (engineered, cofactor).
Compared structures
- 3GWP · Crystal structure of carbon-sulfur lyase involved in aluminum resistance (YP_878183.1)… · 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 A0Q0N1
- Elsewhere: RCSB PDB 3GWP · PDBe 3GWP · UniProt A0Q0N1
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