MolNFT v1 · #115064 · protein

Crystal structure analysis of pp-BRD20 from TB427TMP complexed with bi-2536

5C8G: “Crystal structure analysis of pp-BRD20 from TB427TMP complexed with bi-2536”. X-ray diffraction, 2 ligands (R78, UNX), 2 pockets (best druggability 0.67). MolNFT v1 #115064 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5C8G
Type: protein
Length: 239 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pp-BRD20
UniProt: D0A8L1
Ligands: R78, UNX
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 64% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pp-BRD20	protein	122	61% helix, 0% strand	D0A8L1
B	Pp-BRD20	protein	117	67% helix, 0% strand	D0A8L1

Ligands and binding sites

R78 · 4-{[(7R)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydropteridin-2-yl]amino}-3-methoxy-N-(1-methylpiperidin-4-yl)benzamide · ligand · 2 copies · chains A, B
UNX · Unknown atom or ion · ion · 13 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	481	0.67	0.78	55	empty
2	145	0.53	0.80	23	R78, UNX

Interfaces

1 interface between chains.

A–B · 240 Å² buried · 2 hydrogen bonds · protein-protein

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 D0A8L1
Elsewhere: RCSB PDB 5C8G · PDBe 5C8G · UniProt D0A8L1

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