Research workbench
Arginase I covalently modified with butylamine at Q19C
Analyse Arginase I covalently modified with butylamine at Q19C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZPE
- 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
- MN
- Pockets
- 10 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Arginase 1 (EC 3.5.3.1) | protein | 314 | 42% helix, 16% 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
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 801 | 0.81 | 0.84 | 65 | empty |
| 2 | 246 | 0.57 | 0.78 | 29 | empty |
| 3 | 238 | 0.56 | 0.78 | 29 | empty |
| 4 | 95 | 0.49 | 0.82 | 22 | empty |
| 5 | 86 | 0.46 | 0.81 | 24 | empty |
Interfaces
3 interfaces between chains.
- B–C · 976 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 966 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 938 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (nonstandard).
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 1ZPE · PDBe 1ZPE · UniProt P07824
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