Research workbench
Crystal structure of a putative peptidyl-arginine deiminase
Analyse Crystal structure of a putative peptidyl-arginine deiminase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CMU
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative peptidyl-arginine deiminase
- EC
- 3.5.3.6
- UniProt
- O24890
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative peptidyl-arginine deiminase (EC 3.5.3.6) | protein | 334 | 28% helix, 27% strand | O24890 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.42 | 0.80 | 17 | empty |
| 2 | 63 | 0.37 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2CMU · Crystal structure of a putative peptidyl-arginine deiminase · the same entry in another collection · 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 O24890
- Elsewhere: RCSB PDB 2CMU · PDBe 2CMU · UniProt O24890
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