Research workbench
Room temperature ultra-high resolution time-of-flight neutron and X- ray diffraction studies of H/D exchanged crambin
Analyse Room temperature ultra-high resolution time-of-flight neutron and X- ray… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U7T
- Type
- protein
- Length
- 46 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Crambin
- UniProt
- P01542
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Crambin | protein | 46 | 41% helix, 9% strand | P01542 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3U7T · Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction… · the same entry in another collection · chain A against A, TM-score 1.00
- P01542 · AlphaFold monomer V2.0 prediction for crambin (P01542) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P01542
- Elsewhere: RCSB PDB 3U7T · PDBe 3U7T · UniProt P01542
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