MolNFT v1 · #56297 · protein
Arginase I (homo sapiens): native and unliganded structure at 1.70 a resolution
2ZAV · Arginase-1: “Arginase I (homo sapiens): native and unliganded structure at 1.70 a resolution”. X-ray diffraction, 1 ligand (MN), 4 pockets (best druggability 0.77). MolNFT v1 #56297 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2ZAV
- Type
- protein
- Length
- 621 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
- MN
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginase-1 (EC 3.5.3.1) | protein | 314 | 42% helix, 17% strand | P05089 |
| B | Arginase-1 (EC 3.5.3.1) | protein | 307 | 44% helix, 16% strand | P05089 |
Ligands and binding sites
- 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
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 977 | 0.77 | 0.80 | 92 | empty |
| 2 | 94 | 0.42 | 0.79 | 19 | empty |
| 3 | 59 | 0.33 | 0.77 | 15 | empty |
| 4 | 60 | 0.31 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 476 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2ZAV · Arginase I (homo sapiens): native and unliganded structure at 1.70 A resolution · 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 2ZAV · PDBe 2ZAV · UniProt P05089
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