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2.1 a X-ray structure of cysm (RV1336) from mycobacterium tuberculosis an O-phosphoserine dependent cysteine synthase
Analyse 2.1 a X-ray structure of cysm (RV1336) from mycobacterium tuberculosis an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DKI
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase B
- EC
- 2.5.1.65
- UniProt
- P63873
- Ligands
- NA
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine synthase B (EC 2.5.1.65) | protein | 311 | 41% helix, 19% strand | P63873 |
| B | Cysteine synthase B (EC 2.5.1.65) | protein | 295 | 42% helix, 21% strand | P63873 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.75 | 0.97 | 29 | empty |
| 2 | 580 | 0.70 | 0.79 | 53 | empty |
| 3 | 349 | 0.58 | 0.76 | 48 | empty |
| 4 | 196 | 0.58 | 0.81 | 25 | empty |
| 5 | 69 | 0.31 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 2085 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 3DKI · 2.1 A X-ray structure of CysM (Rv1336) from Mycobacterium tuberculosis an O-phosphoserine… · 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 P63873
- Elsewhere: RCSB PDB 3DKI · PDBe 3DKI · UniProt P63873
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