Research workbench
Ldcorocc mutant- C482A
Analyse Ldcorocc mutant- C482A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ICR
- Type
- protein
- Length
- 193 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coronin-like protein
- UniProt
- Q3T1U8
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 4 distinct chains · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coronin-like protein | protein | 42 | 86% helix, 0% strand | Q3T1U8 |
| B | Coronin-like protein | protein | 53 | 89% helix, 0% strand | Q3T1U8 |
| C | Coronin-like protein | protein | 48 | 90% helix, 0% strand | Q3T1U8 |
| D | Coronin-like protein | protein | 50 | 94% helix, 0% strand | Q3T1U8 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 102 | 0.45 | 0.78 | 17 | empty |
| 2 | 61 | 0.44 | 0.82 | 15 | empty |
Interfaces
6 interfaces between chains.
- B–D · 949 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 838 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 816 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 617 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 392 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6ICR · LdCoroCC mutant- C482A · 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 Q3T1U8
- Elsewhere: RCSB PDB 6ICR · PDBe 6ICR · UniProt Q3T1U8
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