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Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and citrate.
Analyse Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BJK
- Type
- protein
- Length
- 1,032 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-pyrroline-5-carboxylate dehydrogenase
- EC
- 1.5.1.12
- UniProt
- Q5SI02
- Ligands
- NAD, CL
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) | protein | 516 | 42% helix, 21% strand | Q5SI02 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 5 copies · chains A, B
- MRD · (4R)-2-methylpentane-2,4-diol · additive · 4 copies · chains A, B
- FLC · Citrate anion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 610 | 0.81 | 0.86 | 61 | MRD |
| 2 | 809 | 0.78 | 0.81 | 94 | NAD, FLC |
| 3 | 870 | 0.77 | 0.80 | 104 | NAD, FLC, MPD |
| 4 | 407 | 0.67 | 0.80 | 37 | CL |
| 5 | 448 | 0.67 | 0.79 | 41 | CL |
Interfaces
1 interface between chains.
- A–B · 3117 Ų buried · 54 hydrogen bonds · protein-protein
Compared structures
- 2BJK · Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound NAD… · 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 Q5SI02
- Elsewhere: RCSB PDB 2BJK · PDBe 2BJK · UniProt Q5SI02
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