Research workbench
Structure of cystathionine gamma-lyase from pseudomonas aeruginosa
Analyse Structure of cystathionine gamma-lyase from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BA4
- Type
- protein
- Length
- 1,471 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystathionine gamma-lyase
- EC
- 2.5.1.48
- UniProt
- A0A509J8D5
- Ligands
- PLP
- Pockets
- 12 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystathionine gamma-lyase (EC 2.5.1.48) | protein | 377 | 40% helix, 16% strand | A0A509J8D5 |
| B | Cystathionine gamma-lyase (EC 2.5.1.48) | protein | 370 | 40% helix, 17% strand | A0A509J8D5 |
| C | Cystathionine gamma-lyase (EC 2.5.1.48) | protein | 366 | 39% helix, 17% strand | A0A509J8D5 |
| D | Cystathionine gamma-lyase (EC 2.5.1.48) | protein | 358 | 41% helix, 17% strand | A0A509J8D5 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 810 | 0.78 | 0.82 | 97 | PLP |
| 2 | 613 | 0.75 | 0.82 | 81 | PLP |
| 3 | 261 | 0.65 | 0.82 | 48 | PLP |
| 4 | 325 | 0.64 | 0.80 | 47 | PLP |
| 5 | 67 | 0.46 | 0.83 | 14 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2201 Ų buried · 34 hydrogen bonds · protein-protein
- C–D · 2058 Ų buried · 40 hydrogen bonds · protein-protein
- A–C · 1602 Ų buried · 24 hydrogen bonds · protein-protein
- B–D · 1549 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 833 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 7BA4 · Structure of Cystathionine gamma-lyase from Pseudomonas aeruginosa · 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 A0A509J8D5
- Elsewhere: RCSB PDB 7BA4 · PDBe 7BA4 · UniProt A0A509J8D5
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