Research workbench
Crystal structure of the human transglutaminase 1 beta-barrel domain
Analyse Crystal structure of the human transglutaminase 1 beta-barrel domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XZZ
- Type
- protein
- Length
- 97 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-glutamine gamma-glutamyltransferase K
- EC
- 2.3.2.13
- UniProt
- P22735
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-glutamine gamma-glutamyltransferase K (EC 2.3.2.13) | protein | 97 | 4% helix, 45% strand | P22735 |
Compared structures
- 2XZZ · Crystal structure of the human transglutaminase 1 beta-barrel domain · the same entry in another collection · chain A against A, TM-score 1.00
- P22735 · AlphaFold monomer V2.0 prediction for protein-glutamine gamma- glutamyltransferase K… · a predicted model of the same protein · chain A against A, TM-score 0.85
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 P22735
- Elsewhere: RCSB PDB 2XZZ · PDBe 2XZZ · UniProt P22735
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