Research workbench
New protein fold revealed by a 2.3 ångström resolution crystal structure of nerve growth factor
Analyse New protein fold revealed by a 2.3 ångström resolution crystal structure of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BET
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-nerve growth factor
- UniProt
- P01139
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-nerve growth factor | protein | 107 | 0% helix, 61% strand | P01139 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1BET · New protein fold revealed by a 2.3 ångström resolution crystal structure of nerve growth… · the same entry in another collection · chain A against A, TM-score 1.00
- P01139 · AlphaFold monomer V2.0 prediction for beta-nerve growth factor (P01139) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P01139
- Elsewhere: RCSB PDB 1BET · PDBe 1BET · UniProt P01139
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