Research workbench
Joint NMR and X-ray refinement reveals the structure of a novel DIBENZO[A,D]CYCLOHEPTENONE INHIBITOR/P38 MAP kinase complex in solution
Analyse Joint NMR and X-ray refinement reveals the structure of a novel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LGC
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16539
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 359 | — | Q16539 |
Compared structures
- 2LGC · Joint NMR and X-ray refinement reveals the structure of a novel dibenzo[a,d]cyclohepte… · 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 Q16539
- Elsewhere: RCSB PDB 2LGC · PDBe 2LGC · UniProt Q16539
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