MolNFT v1 · #22445 · protein
Arginase-F2-L-arginine complex
1T5G · Arginase 1: “Arginase-F2-L-arginine complex”. X-ray diffraction, 3 ligands (ARG, MN, F), 13 pockets (best druggability 0.81). MolNFT v1 #22445 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1T5G
- Type
- protein
- Length
- 942 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
- ARG, MN, F
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Arginase 1 (EC 3.5.3.1) | protein | 314 | 41% helix, 16% strand | P07824 |
Ligands and binding sites
- ARG · Arginine · ligand · 3 copies · chains A, B, C
- MN · Manganese (II) ion · metal · 6 copies · chains A, B, C
- F · Fluoride ion · ion · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 876 | 0.81 | 0.83 | 69 | empty |
| 2 | 449 | 0.61 | 0.75 | 48 | empty |
| 3 | 179 | 0.58 | 0.82 | 29 | F, ARG |
| 4 | 181 | 0.57 | 0.81 | 29 | F, ARG |
| 5 | 178 | 0.57 | 0.81 | 27 | F, ARG |
Interfaces
3 interfaces between chains.
- B–C · 977 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 956 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 928 Ų buried · 12 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 1T5G · PDBe 1T5G · UniProt P07824
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