Research workbench
Human rabex-5 residues 1-74 in complex with ubiquitin
Analyse Human rabex-5 residues 1-74 in complex with ubiquitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C7M
- Type
- protein
- Length
- 131 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rab guanine nucleotide exchange factor 1; Ubiquitin
- UniProt
- Q53FG0, P62990
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rab guanine nucleotide exchange factor 1 | protein | 58 | 71% helix, 3% strand | Q53FG0 |
| B | Ubiquitin | protein | 73 | 26% helix, 34% strand | P62990 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 749 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2C7M · Human Rabex-5 residues 1-74 in complex with Ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00
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 Q53FG0
- Every structure of UniProt P62990
- Elsewhere: RCSB PDB 2C7M · PDBe 2C7M · UniProt Q53FG0 · UniProt P62990
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