Research workbench
Crystal structure of S-nitrosylated nitrosoglutathione REDUCTASE(GSNOR)FROM chlamydomonas reinhardtii, in complex with NAD+
Analyse Crystal structure of S-nitrosylated nitrosoglutathione REDUCTASE(GSNOR)FROM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AV7
- Type
- protein
- Length
- 2,259 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-(HYDROXYMETHYL)GLUTATHIONE dehydrogenase
- EC
- 1.1.1.284
- UniProt
- A0A2K3D6R4
- Ligands
- NAD, ZN, CL
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F | S-(HYDROXYMETHYL)GLUTATHIONE dehydrogenase (EC 1.1.1.284) | protein | 377 | 31% helix, 25% strand | A0A2K3D6R4 |
| E | S-(HYDROXYMETHYL)GLUTATHIONE dehydrogenase (EC 1.1.1.284) | protein | 374 | 30% helix, 26% strand | A0A2K3D6R4 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 6 copies · chains A, F, B, C, D, E
- ZN · Zinc ion · metal · 12 copies · chains A, B, C, D, E, F
- CL · Chloride ion · ion · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 998 | 0.82 | 0.83 | 102 | empty |
| 2 | 1131 | 0.82 | 0.83 | 133 | NAD |
| 3 | 971 | 0.80 | 0.81 | 89 | NAD |
| 4 | 1044 | 0.78 | 0.80 | 94 | NAD |
| 5 | 956 | 0.78 | 0.80 | 72 | NAD |
Interfaces
7 interfaces between chains.
- D–E · 1741 Ų buried · 25 hydrogen bonds · protein-protein
- A–F · 1741 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 1730 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 491 Ų buried · 6 hydrogen bonds · protein-protein
- D–F · 370 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 2 covalent (nonstandard, covalent ligand).
Compared structures
- 7AV7 · Crystal structure of S-nitrosylated nitrosoglutathione reductase(GSNOR)from Chlamydomonas… · 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 A0A2K3D6R4
- Elsewhere: RCSB PDB 7AV7 · PDBe 7AV7 · UniProt A0A2K3D6R4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.