MolNFT v1 · #161916 · protein

Crystal structure of the SIR4 H-brct domain in complex with ESC1 PS1450 peptide

6QSZ · Regulatory protein SIR4: “Crystal structure of the SIR4 H-brct domain in complex with ESC1 PS1450 peptide”. X-ray diffraction, 1 ligand (CL), 15 pockets (best druggability 0.78). MolNFT v1 #161916 on GenesisL1: 3D structure, binding…

PDB: 6QSZ
Type: protein
Length: 978 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulatory protein SIR4; Silent chromatin protein ESC1
UniProt: P11978, Q03661
Ligands: CL
Pockets: 15 · best druggability 0.78

Structure

x-ray diffraction · 12 distinct chains · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Regulatory protein SIR4	protein	112	52% helix, 13% strand	P11978
B, D, F	Silent chromatin protein ESC1	protein	9	0% helix, 0% strand	Q03661
C	Regulatory protein SIR4	protein	113	53% helix, 11% strand	P11978
E	Regulatory protein SIR4	protein	113	53% helix, 11% strand	P11978
G	Regulatory protein SIR4	protein	114	52% helix, 11% strand	P11978
H	Silent chromatin protein ESC1	protein	11	0% helix, 0% strand	Q03661
I	Regulatory protein SIR4	protein	112	53% helix, 11% strand	P11978
J	Silent chromatin protein ESC1	protein	7	0% helix, 0% strand	Q03661
K	Regulatory protein SIR4	protein	114	54% helix, 11% strand	P11978
L, N, P	Silent chromatin protein ESC1	protein	10	0% helix, 0% strand	Q03661
M	Regulatory protein SIR4	protein	114	50% helix, 11% strand	P11978
O	Regulatory protein SIR4	protein	111	52% helix, 12% strand	P11978

Ligands and binding sites

CL · Chloride ion · ion · chains C, G

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	537	0.78	0.85	37	empty
2	725	0.73	0.79	61	empty
3	599	0.69	0.78	43	CL
4	416	0.62	0.77	34	empty
5	357	0.58	0.76	36	empty

Interfaces

24 interfaces between chains.

C–G · 754 Å² buried · 15 hydrogen bonds · protein-protein
G–K · 749 Å² buried · 14 hydrogen bonds · protein-protein
C–E · 730 Å² buried · 14 hydrogen bonds · protein-protein
G–H · 554 Å² buried · 14 hydrogen bonds · protein-protein
M–N · 552 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 40 modified (engineered, phosphorylation).

Compared structures

6QSZ · Crystal structure of the Sir4 H-BRCT domain in complex with Esc1 pS1450 peptide · the same entry in another collection · chain G against G, 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 P11978
Every structure of UniProt Q03661
Elsewhere: RCSB PDB 6QSZ · PDBe 6QSZ · UniProt P11978 · UniProt Q03661

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