Research workbench
The structure of cysteine synthase from mycobacterium ulcerans AGY99
Analyse The structure of cysteine synthase from mycobacterium ulcerans AGY99 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I1Y
- Type
- protein
- Length
- 1,065 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase
- EC
- 2.5.1.47
- UniProt
- A0PNS1
- Ligands
- CL, SO4
- Pockets
- 6 · best druggability 0.64
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine synthase (EC 2.5.1.47) | protein | 263 | 44% helix, 19% strand | A0PNS1 |
| B | Cysteine synthase (EC 2.5.1.47) | protein | 264 | 44% helix, 20% strand | A0PNS1 |
| C | Cysteine synthase (EC 2.5.1.47) | protein | 268 | 44% helix, 19% strand | A0PNS1 |
| D | Cysteine synthase (EC 2.5.1.47) | protein | 270 | 41% helix, 20% strand | A0PNS1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.64 | 0.75 | 71 | empty |
| 2 | 400 | 0.61 | 0.76 | 43 | empty |
| 3 | 56 | 0.46 | 0.84 | 18 | empty |
| 4 | 109 | 0.40 | 0.75 | 15 | empty |
| 5 | 93 | 0.36 | 0.75 | 18 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1678 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1553 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 263 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4I1Y · The structure of Cysteine synthase from Mycobacterium ulcerans Agy99 · 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 A0PNS1
- Elsewhere: RCSB PDB 4I1Y · PDBe 4I1Y · UniProt A0PNS1
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