MolNFT v1 · #62212 · protein
X-ray structure of rat arginase I-N130A mutant: the unliganded complex
3E8Z · Arginase-1: “X-ray structure of rat arginase I-N130A mutant: the unliganded complex”. X-ray diffraction, 1 ligand (MN), 9 pockets (best druggability 0.82). MolNFT v1 #62212 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3E8Z
- Type
- protein
- Length
- 924 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginase-1
- EC
- 3.5.3.1
- UniProt
- P07824
- Ligands
- MN
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Arginase-1 (EC 3.5.3.1) | protein | 308 | 42% helix, 18% strand | P07824 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1108 | 0.82 | 0.83 | 92 | empty |
| 2 | 215 | 0.54 | 0.78 | 31 | empty |
| 3 | 217 | 0.53 | 0.77 | 28 | empty |
| 4 | 124 | 0.51 | 0.81 | 25 | MN |
| 5 | 119 | 0.50 | 0.81 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–C · 776 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 758 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 735 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
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 P07824
- Elsewhere: RCSB PDB 3E8Z · PDBe 3E8Z · UniProt P07824
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.