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NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure
Analyse NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TRL
- Type
- protein
- Length
- 124 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermolysin fragment 255 - 316
- EC
- 3.4.24.27
- UniProt
- P00800
Structure
solution nmr · 1 distinct chain · 66% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thermolysin fragment 255 - 316 (EC 3.4.24.27) | protein | 62 | 66% helix, 2% strand | P00800 |
Interfaces
1 interface between chains.
- A–B · 1317 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1TRL · NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed… · 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 P00800
- Elsewhere: RCSB PDB 1TRL · PDBe 1TRL · UniProt P00800
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