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Crystal structure of human C1ORF123 protein
Analyse Crystal structure of human C1ORF123 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZRT
- Type
- protein
- Length
- 320 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UPF0587 protein C1ORF123
- UniProt
- Q9NWV4
- Ligands
- ZN, CL
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | UPF0587 protein C1ORF123 | protein | 160 | 6% helix, 57% strand | Q9NWV4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 6 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.69 | 0.96 | 20 | empty |
| 2 | 241 | 0.51 | 0.75 | 30 | empty |
| 3 | 244 | 0.50 | 0.75 | 31 | empty |
| 4 | 101 | 0.46 | 0.80 | 23 | GOL |
| 5 | 52 | 0.37 | 0.80 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 595 Ų buried · 8 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 Q9NWV4
- Elsewhere: RCSB PDB 5ZRT · PDBe 5ZRT · UniProt Q9NWV4
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