MolNFT v2 · #220373 · protein

Copper Complex of Peanut USP-type BURP Domain Peptide Cyclase

8SY3 · BURP domain-containing protein: “Copper Complex of Peanut USP-type BURP Domain Peptide Cyclase”. X-ray diffraction at 3.2, 1 ligand (CU), 7 pockets (best druggability 0.54). MolNFT v2 #220373 on GenesisL1: 3D structure, binding…

PDB: 8SY3
Type: protein
Length: 409 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.2
Source: Arachis hypogaea
Molecule: BURP domain-containing protein
UniProt: A0A445DYW3
Ligands: CU
Pockets: 7 · best druggability 0.54

Structure

x-ray diffraction · resolution 3.2 · 2 distinct chains · 22% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BURP domain-containing protein	protein	209	22% helix, 30% strand	A0A445DYW3
B	BURP domain-containing protein	protein	200	23% helix, 32% strand	A0A445DYW3

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	267	0.54	0.76	46	empty
2	255	0.52	0.75	35	empty
3	163	0.50	0.78	21	empty
4	110	0.43	0.77	23	empty
5	124	0.40	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 921 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

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 A0A445DYW3
Elsewhere: RCSB PDB 8SY3 · PDBe 8SY3 · UniProt A0A445DYW3

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