MolNFT v1 · #152479 · protein

Crystal structure of human UHRF1 phd finger in complex with PAF15

6IIW · E3 ubiquitin-protein ligase UHRF1: “Crystal structure of human UHRF1 phd finger in complex with PAF15”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #152479 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6IIW · Crystal structure of human UHRF1 PHD finger in complex with PAF15 · the same entry in another collection · chain A against A, TM-score 1.00
Q15004 · AlphaFold monomer V2.0 prediction for PCNA-associated factor (Q15004) · a predicted model of the same protein · chain B against A, TM-score 0.62

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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