5BZX
Crystal structure of human phosphatase PTEN treated with a bisperoxovanadium complex
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B, C, D (A, B, C, D) | Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN | polymer | 314 | 37307.8 | 4 | UniProt (P60484) Pfam (PF22785) Pfam (PF10409) | Homo sapiens (Human) | Mutated in multiple advanced cancers 1,Phosphatase and tensin homolog |
2 | E, H (A, C) | VANADATE ION | non-polymer | 114.9 | 2 | Chemie (VO4) | |||
3 | F, G, I (B, C, D) | L(+)-TARTARIC ACID | non-polymer | 150.1 | 3 | Chemie (TLA) | |||
4 | J, K, L, M (A, B, C, D) | water | water | 18.0 | 880 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 14 - 351 (UniProt: P60484)
PDB | External Database | Details |
---|---|---|
- | Thr 286 | deletion |
- | Ser 287 | deletion |
- | Glu 288 | deletion |
- | Lys 289 | deletion |
- | Val 290 | deletion |
- | Glu 291 | deletion |
- | Asn 292 | deletion |
- | Gly 293 | deletion |
- | Ser 294 | deletion |
- | Leu 295 | deletion |
- | Cys 296 | deletion |
- | Asp 297 | deletion |
- | Gln 298 | deletion |
- | Glu 299 | deletion |
- | Ile 300 | deletion |
- | Asp 301 | deletion |
- | Ser 302 | deletion |
- | Ile 303 | deletion |
- | Cys 304 | deletion |
- | Ser 305 | deletion |
- | Ile 306 | deletion |
- | Glu 307 | deletion |
- | Arg 308 | deletion |
- | Ala 309 | deletion |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 149231.2 | |
Non-Polymers* | Number of molecules | 5 |
Total formula weight | 680.1 | |
All* | Total formula weight | 149911.4 |