Research workbench
Structure of the cak complex form chaetomium thermophilum
Analyse Structure of the cak complex form chaetomium thermophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z3U
- Type
- protein
- Length
- 1,404 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G0SH78, G0SFC6, G0SF48
- Ligands
- CL
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 312 | — | G0SH78 |
| B | — | protein | 322 | — | G0SFC6 |
| C | — | protein | 66 | — | G0SF48 |
| D | — | protein | 314 | — | G0SH78 |
| E | — | protein | 323 | — | G0SFC6 |
| F | — | protein | 67 | — | G0SF48 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6Z3U · Structure of the CAK complex form Chaetomium thermophilum · 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 G0SH78
- Every structure of UniProt G0SFC6
- Every structure of UniProt G0SF48
- Elsewhere: RCSB PDB 6Z3U · PDBe 6Z3U · UniProt G0SH78 · UniProt G0SFC6 · UniProt G0SF48
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