MolNFT v1 · #135237 · protein
Inactive conformation of engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine
5TT2 · Cystathionine gamma-lyase: “Inactive conformation of engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting…”. X-ray diffraction, 1 ligand (SO4), 6 pockets (best druggability 0.77). MolNFT v1 #135237 on…
- PDB
- 5TT2
- Type
- protein
- Length
- 686 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystathionine gamma-lyase
- EC
- 4.4.1.1
- UniProt
- P32929
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | Cystathionine gamma-lyase (EC 4.4.1.1) | protein | 343 | 40% helix, 17% strand | P32929 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 630 | 0.77 | 0.82 | 67 | SO4 |
| 2 | 562 | 0.77 | 0.83 | 67 | SO4 |
| 3 | 168 | 0.58 | 0.82 | 22 | empty |
| 4 | 269 | 0.52 | 0.75 | 34 | empty |
| 5 | 63 | 0.31 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- C–D · 1061 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 5TT2 · Inactive conformation of engineered human cystathionine gamma lyase (E59N, R119L, E339V)… · the same entry in another collection · chain C against C, TM-score 1.00
- P32929 · AlphaFold monomer V2.0 prediction for cystathionine gamma-lyase (P32929) · a predicted model of the same protein · chain D against A, TM-score 0.95
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 P32929
- Elsewhere: RCSB PDB 5TT2 · PDBe 5TT2 · UniProt P32929
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