Research workbench
Crystal structure of human UHRF1 phd finger in complex with PAF15
Analyse Crystal structure of human UHRF1 phd finger in complex with PAF15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IIW
- Type
- protein
- Length
- 72 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1; PCNA-associated factor
- EC
- 2.3.2.27
- UniProt
- Q96T88, Q15004
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) | protein | 66 | 5% helix, 11% strand | Q96T88 |
| B | PCNA-associated factor | protein | 6 | 0% helix, 17% strand | Q15004 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 437 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 Q96T88
- Every structure of UniProt Q15004
- Elsewhere: RCSB PDB 6IIW · PDBe 6IIW · UniProt Q96T88 · UniProt Q15004
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