6ML1
Structure of the USP15 deubiquitinase domain in complex with an affinity-matured inhibitory Ubv
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B (A, B) | Ubiquitin carboxyl-terminal hydrolase 15,Ubiquitin carboxyl-terminal hydrolase 15,Ubiquitin carboxyl-terminal hydrolase 15 | polymer | 349 | 39753.0 | 2 | UniProt (Q9Y4E8) Pfam (PF00443) | Homo sapiens (Human) | Deubiquitinating enzyme 15,Ubiquitin thioesterase 15,Ubiquitin-specific-processing protease 15,Unph-2,Unph4,Deubiquitinating enzyme 15,Ubiquitin thioesterase 15,Ubiquitin-specific-processing protease 15,Unph-2,Unph4,Deubiquitinating enzyme 15,Ubiquitin thioesterase 15,Ubiquitin-specific-processing protease 15,Unph-2,Unph4 |
2 | C, D (E, C) | Ubiquitin variant 15.1a | polymer | 92 | 10282.8 | 2 | UniProt (A0A0L7RG06) Pfam (PF00240) | Homo sapiens | |
3 | E (G) | Proteolyzed N-terminal tag of Ubv.15.1a construct | polymer | 26 | 3055.3 | 1 | Escherichia coli | ||
4 | F, G, K, Q (A, B, C) | CALCIUM ION | non-polymer | 40.1 | 4 | Chemie (CA) | |||
5 | H, L (A, B) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
6 | I, J, O, P (A, B) | SODIUM ION | non-polymer | 23.0 | 4 | Chemie (NA) | |||
7 | M (B) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 1 | Chemie (EDO) | |||
8 | N (B) | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
9 | R (C) | 2-(N-MORPHOLINO)-ETHANESULFONIC ACID | non-polymer | 195.2 | 1 | Chemie (MES) | |||
10 | S, T, U, V, W (A, B, E, C, G) | water | water | 18.0 | 389 | Chemie (HOH) |
Sequence modifications
A, B: 275 - 470 (UniProt: Q9Y4E8)
A, B: 781 - 862 (UniProt: Q9Y4E8)
A, B: 873 - 934 (UniProt: Q9Y4E8)
E, C: -2 - 82 (UniProt: A0A0L7RG06)
PDB | External Database | Details |
---|---|---|
Ser 270 | - | expression tag |
Gly 271 | - | expression tag |
Ala 272 | - | expression tag |
Ala 273 | - | expression tag |
Ala 274 | - | expression tag |
A, B: 873 - 934 (UniProt: Q9Y4E8)
PDB | External Database | Details |
---|---|---|
Gly 872 | - | linker |
Ser 935 | - | expression tag |
Ser 936 | - | expression tag |
Gly 937 | - | expression tag |
PDB | External Database | Details |
---|---|---|
Ala -1 | - | insertion |
Ala 0 | Gly 380 | conflict |
Leu 2 | Gln 382 | conflict |
Ser 9 | Thr 389 | conflict |
Phe 12 | Thr 392 | conflict |
Ser 14 | Thr 394 | conflict |
Pro 19 | Ala 399 | conflict |
- | Asp 427 | deletion |
Gly 47 | Gln 428 | conflict |
Lys 48 | Gln 429 | conflict |
Ser 51 | Ile 432 | conflict |
Tyr 53 | Ala 434 | conflict |
Arg 54 | Gly 435 | conflict |
His 71 | Glu 452 | conflict |
Gln 75 | His 456 | conflict |
Leu 77 | Val 458 | conflict |
Val 78 | Leu 459 | conflict |
Ile 79 | Arg 460 | conflict |
Ser 80 | Leu 461 | conflict |
Ile 83 | - | expression tag |
Leu 84 | - | expression tag |
Tyr 85 | - | expression tag |
Gly 86 | - | expression tag |
Ser 87 | - | expression tag |
Ser 88 | - | expression tag |
Gly 89 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 5 |
Total formula weight | 103127.1 | |
Non-Polymers* | Number of molecules | 13 |
Total formula weight | 675.8 | |
All* | Total formula weight | 103802.9 |