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Crystal structure of the CO2+2-human arginase I-agpa complex
Analyse Crystal structure of the CO2+2-human arginase I-agpa complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FCK
- Type
- protein
- Length
- 628 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
- GPA, CO
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Arginase-1 (EC 3.5.3.1) | protein | 314 | 42% helix, 17% strand | P05089 |
Ligands and binding sites
- GPA · 2-amino-3-guanidino-propionic acid · ligand · 2 copies · chains A, B
- CO · Cobalt (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 923 | 0.76 | 0.79 | 94 | GPA |
| 2 | 86 | 0.39 | 0.78 | 19 | GPA |
| 3 | 51 | 0.36 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 462 Ų buried · 2 hydrogen bonds · 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 4FCK · PDBe 4FCK · UniProt P05089
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