Research workbench
Crystal structure of malonyl-CoA decarboxylase from agrobacterium vitis, northeast structural genomics consortium target RIR35
Analyse Crystal structure of malonyl-CoA decarboxylase from agrobacterium vitis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KSF
- Type
- protein
- Length
- 407 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Malonyl-CoA decarboxylase
- UniProt
- B9K0V9
- Ligands
- NI, CL
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Malonyl-CoA decarboxylase | protein | 407 | 46% helix, 12% strand | B9K0V9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.56 | 0.77 | 45 | empty |
| 2 | 86 | 0.47 | 0.81 | 17 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4KSF · Crystal Structure of Malonyl-CoA decarboxylase from Agrobacterium vitis, Northeast… · 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 B9K0V9
- Elsewhere: RCSB PDB 4KSF · PDBe 4KSF · UniProt B9K0V9
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