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Crystal structure of the C-terminal fragment (426-558) lamin-B1 from homo sapiens, northeast structural genomics consortium target HR5546A
Analyse Crystal structure of the C-terminal fragment (426-558) lamin-B1 from homo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JT0
- Type
- protein
- Length
- 215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lamin-B1
- UniProt
- P20700
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lamin-B1 | protein | 107 | 0% helix, 47% strand | P20700 |
| B | Lamin-B1 | protein | 108 | 0% helix, 45% strand | P20700 |
Interfaces
1 interface between chains.
- A–B · 486 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3JT0 · Crystal Structure of the C-terminal fragment (426-558) Lamin-B1 from Homo sapiens… · the same entry in another collection · chain A against A, TM-score 1.00
- P20700 · AlphaFold monomer V2.0 prediction for lamin-B1 (P20700) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P20700
- Elsewhere: RCSB PDB 3JT0 · PDBe 3JT0 · UniProt P20700
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