MolNFT v1 · #133094 · protein
Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function
5RLA: “Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function”. X-ray diffraction, 1 ligand (MN), 12 pockets (best druggability 0.79). MolNFT v1 #133094 on GenesisL1: 3D structure, binding…
- PDB
- 5RLA
- Type
- protein
- Length
- 942 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginase
- EC
- 3.5.3.1
- UniProt
- P07824
- Ligands
- MN
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Arginase (EC 3.5.3.1) | protein | 314 | 41% helix, 15% strand | P07824 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1181 | 0.79 | 0.81 | 94 | empty |
| 2 | 207 | 0.53 | 0.78 | 28 | empty |
| 3 | 198 | 0.51 | 0.77 | 29 | empty |
| 4 | 98 | 0.48 | 0.81 | 22 | empty |
| 5 | 110 | 0.47 | 0.80 | 23 | empty |
Interfaces
3 interfaces between chains.
- B–C · 968 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 956 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 938 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5RLA · Altering the binuclear manganese cluster of arginase diminishes thermostability and… · the same entry in another collection · chain A against A, TM-score 1.00
- P07824 · AlphaFold monomer V2.0 prediction for arginase-1 (P07824) · 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 P07824
- Elsewhere: RCSB PDB 5RLA · PDBe 5RLA · UniProt P07824
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