MolNFT v1 · #126140 · protein

Complex of human 14-3-3 sigma CLU1 mutant with phosphorylated heat shock protein B6

5LTW · 14-3-3 protein sigma: “Complex of human 14-3-3 sigma CLU1 mutant with phosphorylated heat shock protein B6”. X-ray diffraction, 1 ligand (NI), 20 pockets (best druggability 0.78). MolNFT v1 #126140 on GenesisL1: 3D structure…

PDB: 5LTW
Type: protein
Length: 2,011 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein sigma; Heat shock protein beta-6
UniProt: P31947, O14558
Ligands: NI
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 10 distinct chains · 58% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein sigma	protein	227	83% helix, 0% strand	P31947
B	14-3-3 protein sigma	protein	226	83% helix, 0% strand	P31947
C	Heat shock protein beta-6	protein	113	5% helix, 48% strand	O14558
D, H	Heat shock protein beta-6	protein	98	6% helix, 53% strand	O14558
E	14-3-3 protein sigma	protein	227	83% helix, 0% strand	P31947
F, J	14-3-3 protein sigma	protein	229	83% helix, 0% strand	P31947
G	Heat shock protein beta-6	protein	118	5% helix, 45% strand	O14558
I	14-3-3 protein sigma	protein	232	81% helix, 0% strand	P31947
K	Heat shock protein beta-6	protein	114	5% helix, 46% strand	O14558
L	Heat shock protein beta-6	protein	100	6% helix, 46% strand	O14558

Ligands and binding sites

NI · Nickel (II) ion · metal · 3 copies · chains D, H, L
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 6 copies · chains A, B, E, F, I, J

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1040	0.78	0.80	85	empty
2	710	0.69	0.76	78	empty
3	447	0.68	0.80	42	empty
4	446	0.67	0.79	46	empty
5	77	0.66	0.92	22	empty

Interfaces

18 interfaces between chains.

F–G · 1163 Å² buried · 23 hydrogen bonds · protein-protein
D–H · 1146 Å² buried · 17 hydrogen bonds · protein-protein
J–K · 1065 Å² buried · 22 hydrogen bonds · protein-protein
I–J · 1039 Å² buried · 16 hydrogen bonds · protein-protein
G–H · 1027 Å² buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (phosphorylation).

Compared structures

5LTW · Complex of human 14-3-3 sigma CLU1 mutant with phosphorylated heat shock protein B6 · the same entry in another collection · chain L against L, 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 P31947
Every structure of UniProt O14558
Elsewhere: RCSB PDB 5LTW · PDBe 5LTW · UniProt P31947 · UniProt O14558

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