MolNFT v1 · #147521 · protein

Crystal structure of the human chip tpr domain in complex with a 5MER acetylated HSP70 peptide

6EFK · E3 ubiquitin-protein ligase chip: “Crystal structure of the human chip tpr domain in complex with a 5MER acetylated HSP70 peptide”. X-ray diffraction, 2 ligands (ACE, NA), 1 pocket (best druggability 0.78). MolNFT v1 #147521 on…

PDB: 6EFK
Type: protein
Length: 274 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase chip; ACE-ile-glu-glu-val-asp
EC: 2.3.2.27
UniProt: Q9UNE7
Ligands: ACE, NA
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	E3 ubiquitin-protein ligase chip (EC 2.3.2.27)	protein	132	77% helix, 0% strand	Q9UNE7
C, D	ACE-ile-glu-glu-val-asp	protein	5	0% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 2 copies · chains A, B, C, D
NA · Sodium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	687	0.78	0.83	65	empty

Interfaces

5 interfaces between chains.

A–B · 722 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 527 Å² buried · 10 hydrogen bonds · protein-protein
A–D · 516 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 18 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 18 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

6EFK · Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated HSP70… · the same entry in another collection · chain A against A, TM-score 1.00
Q9UNE7 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase chip (Q9UNE7) · a predicted model of the same protein · chain A 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 Q9UNE7
Elsewhere: RCSB PDB 6EFK · PDBe 6EFK · UniProt Q9UNE7

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