MolNFT v2 · #105983 · protein
Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function
4RLA: “Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function”. X-ray diffraction at 2.94. MolNFT v2 #105983 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4RLA
- Type
- protein
- Length
- 942 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.94
- Source
- Rattus norvegicus
- UniProt
- P07824
Structure
x-ray diffraction · resolution 2.94 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 314 | — | P07824 |
Compared structures
- 4RLA · 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 A 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 4RLA · PDBe 4RLA · UniProt P07824
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