MolNFT v1 · #62133 · protein
X-ray structure of human arginase I: the mutant D183A in complex with abh
3E6K · Arginase-1: “X-ray structure of human arginase I: the mutant D183A in complex with abh”. X-ray diffraction, 2 ligands (ABH, MN), 5 pockets (best druggability 0.72). MolNFT v1 #62133 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3E6K
- Type
- protein
- Length
- 616 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
- ABH, MN
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Arginase-1 (EC 3.5.3.1) | protein | 308 | 42% helix, 16% strand | P05089 |
Ligands and binding sites
- ABH · 2(S)-amino-6-boronohexanoic acid · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 991 | 0.72 | 0.76 | 84 | ABH |
| 2 | 64 | 0.42 | 0.81 | 14 | empty |
| 3 | 99 | 0.41 | 0.78 | 20 | ABH |
| 4 | 75 | 0.38 | 0.77 | 16 | empty |
| 5 | 68 | 0.30 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 290 Ų buried · 1 hydrogen bond · 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 P05089
- Elsewhere: RCSB PDB 3E6K · PDBe 3E6K · UniProt P05089
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