Research workbench
CA2+-bound D184N mutant mthk rck domain at 2.4 ångström
Analyse CA2+-bound D184N mutant mthk rck domain at 2.4 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L75
- Type
- protein
- Length
- 1,341 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O27564
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 229 | — | O27564 |
| B | — | protein | 224 | — | O27564 |
| C, E | — | protein | 221 | — | O27564 |
| D, F | — | protein | 223 | — | O27564 |
Compared structures
- 4L75 · Ca2+-bound D184N mutant MthK RCK domain at 2.4 Angstrom · 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 O27564
- Elsewhere: RCSB PDB 4L75 · PDBe 4L75 · UniProt O27564
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