Research workbench
Structure of N-terminus locked esp with one pro-peptide residue - V67C, D255C
Analyse Structure of N-terminus locked esp with one pro-peptide residue - V67C, D255C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TYA
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamyl endopeptidase
- EC
- 3.4.21.19
- UniProt
- P0C0Q2
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamyl endopeptidase (EC 3.4.21.19) | protein | 217 | 13% helix, 41% strand | P0C0Q2 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6TYA · Structure of N-terminus locked Esp with one pro-peptide residue - V67C, D255C · the same entry in another collection · chain A against A, TM-score 1.00
- P0C0Q2 · AlphaFold monomer V2.0 prediction for glutamyl endopeptidase (P0C0Q2) · a predicted model of the same protein · 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 P0C0Q2
- Elsewhere: RCSB PDB 6TYA · PDBe 6TYA · UniProt P0C0Q2
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