Research workbench
Crystal structure of human RANGAP1-UBC9
Analyse Crystal structure of human RANGAP1-UBC9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GRN
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-conjugating enzyme E2 I; Ran GTPase-activating protein 1
- EC
- 6.3.2.19
- UniProt
- P63279, P46060
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-conjugating enzyme E2 I (EC 6.3.2.19) | protein | 157 | 35% helix, 20% strand | P63279 |
| B | Ran GTPase-activating protein 1 | protein | 157 | 63% helix, 0% strand | P46060 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.46 | 0.78 | 17 | empty |
| 2 | 107 | 0.36 | 0.74 | 23 | empty |
| 3 | 70 | 0.29 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 589 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2GRN · Crystal Structure of human RanGAP1-Ubc9 · the same entry in another collection · chain A against A, TM-score 1.00
- P46060 · AlphaFold monomer V2.0 prediction for ran GTPase-activating protein 1 (P46060) · a predicted model of the same protein · chain B against A, TM-score 0.99
- 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 0.99
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 P46060
- Elsewhere: RCSB PDB 2GRN · PDBe 2GRN · UniProt P63279 · UniProt P46060
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