MolNFT v2 · #151138 · protein
Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft of microbial transglutaminase
6GMG: “Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft of microbial…”. X-ray diffraction at 2.25. MolNFT v2 #151138 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GMG
- Type
- protein
- Length
- 678 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.25
- Source
- Streptomyces mobaraensis NBRC 13819 = DSM 40847; SYNTHETIC CONSTRUCT
- UniProt
- M3C567
Structure
x-ray diffraction · resolution 2.25 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 331 | — | M3C567 |
| B | — | protein | 330 | — | M3C567 |
| C | — | protein | 8 | — | — |
| D | — | protein | 9 | — | — |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B
- FLC · Citrate anion · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GMG · Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft… · 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 M3C567
- Elsewhere: RCSB PDB 6GMG · PDBe 6GMG · UniProt M3C567
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