1L9N
Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | Protein-glutamine glutamyltransferase E3 | polymer | 692 | 76670.5 | 2 | UniProt (Q08188) Pfam (PF00868) Pfam (PF01841) Pfam (PF00927) In PDB | Homo sapiens (human) | Transglutaminase 3, TGM3, TGASE E3 |
| 2 | A, B | 2-O-octyl-beta-D-glucopyranose | non-polymer | 292.4 | 2 | Chemie (BGL) | |||
| 3 | A, B | CALCIUM ION | non-polymer | 40.1 | 6 | Chemie (CA) | |||
| 4 | A, B | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
| 5 | water | water | 18.0 | 1013 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 692 (UniProt: Q08188)
| PDB | External Database | Details |
|---|---|---|
| Asp 250 | Asn 251 | SEE REMARK 999 |
| Leu 264 | Phe 265 | engineered mutation |
| Arg 561 | Lys 562 | SEE REMARK 999 |
| Arg 653 | Gly 654 | SEE REMARK 999 |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 153341.0 | |
| Non-Polymers* | Number of molecules | 10 |
| Total formula weight | 896.1 | |
| All* | Total formula weight | 154237.1 |
