MolNFT v1 · #98575 · protein

Crystal structure of CPBRD2 from cryptosporidium, CGD3_3190

4LDF · GCN5 like acetylase + bromodomain: “Crystal structure of CPBRD2 from cryptosporidium, CGD3_3190”. X-ray diffraction, 1 ligand (UNX), 3 pockets (best druggability 0.55). MolNFT v1 #98575 on GenesisL1: 3D structure, binding sites and…

PDB: 4LDF
Type: protein
Length: 213 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GCN5 like acetylase + bromodomain
UniProt: Q5CUE2
Ligands: UNX
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GCN5 like acetylase + bromodomain	protein	107	64% helix, 0% strand	Q5CUE2
B	GCN5 like acetylase + bromodomain	protein	106	65% helix, 0% strand	Q5CUE2

Ligands and binding sites

UNX · Unknown atom or ion · ion · chains B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

3 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	135	0.55	0.82	20	GOL
2	322	0.55	0.75	22	empty
3	137	0.54	0.81	20	GOL

Interfaces

1 interface between chains.

A–B · 85 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4LDF · Crystal Structure of CpBRD2 from cryptosporidium, cgd3_3190 · 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 Q5CUE2
Elsewhere: RCSB PDB 4LDF · PDBe 4LDF · UniProt Q5CUE2

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