Research workbench
Crystal structure of human arginase I in complex with L-2- aminohistidine and sulphate
Analyse Crystal structure of human arginase I in complex with L-2- aminohistidine and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MFW
- Type
- protein
- Length
- 629 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginase-1
- EC
- 3.5.3.1
- UniProt
- P05089
- Ligands
- B3U, MN, SO4
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginase-1 (EC 3.5.3.1) | protein | 315 | 42% helix, 17% strand | P05089 |
| B | Arginase-1 (EC 3.5.3.1) | protein | 314 | 43% helix, 17% strand | P05089 |
Ligands and binding sites
- B3U · 2-amino-L-histidine · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
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 | 973 | 0.78 | 0.80 | 94 | SO4, B3U |
| 2 | 86 | 0.42 | 0.80 | 19 | SO4, B3U |
Interfaces
1 interface between chains.
- A–B · 460 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3MFW · Crystal structure of human arginase I in complex with L-2-aminohistidine and sulphate · the same entry in another collection · chain A against A, TM-score 1.00
- P05089 · AlphaFold monomer V2.0 prediction for arginase-1 (P05089) · a predicted model of the same protein · chain B 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 P05089
- Elsewhere: RCSB PDB 3MFW · PDBe 3MFW · UniProt P05089
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.