MolNFT v1 · #119241 · protein
Crystal structure of human sumo E1 ufd domain in complex with UBC9 in a P422 space group.
5FQ2 · Sumo-conjugating enzyme UBC9: “Crystal structure of human sumo E1 ufd domain in complex with UBC9 in a P422 space group.”. X-ray diffraction, 1 pocket (best druggability 0.63). MolNFT v1 #119241 on GenesisL1: 3D structure, binding…
- PDB
- 5FQ2
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sumo-conjugating enzyme UBC9; Sumo-activating enzyme subunit 2
- EC
- 6.3.2.-
- UniProt
- P63279, Q9UBT2
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sumo-conjugating enzyme UBC9 (EC 6.3.2.-) | protein | 157 | 35% helix, 20% strand | P63279 |
| B | Sumo-activating enzyme subunit 2 (EC 6.3.2.-) | protein | 101 | 19% helix, 34% strand | Q9UBT2 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.63 | 0.93 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 787 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation, nonstandard).
Compared structures
- 5FQ2 · Crystal structure of human SUMO E1 UFD domain in complex with Ubc9 in a P422 space group. · the same entry in another collection · chain A against A, TM-score 1.00
- P63279 · AlphaFold monomer V2.0 prediction for sumo-conjugating enzyme UBC9 (P63279) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q9UBT2 · AlphaFold monomer V2.0 prediction for sumo-activating enzyme subunit 2 (Q9UBT2) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P63279
- Every structure of UniProt Q9UBT2
- Elsewhere: RCSB PDB 5FQ2 · PDBe 5FQ2 · UniProt P63279 · UniProt Q9UBT2
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