MolNFT v1 · #128631 · protein

14-3-3C in complex with cpp and fusicoccin

5NWK · 14-3-3 C-1 protein: “14-3-3C in complex with cpp and fusicoccin”. X-ray diffraction, 2 ligands (FSC, SEP), 20 pockets (best druggability 0.80). MolNFT v1 #128631 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5NWK
Type: protein
Length: 1,908 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 C-1 protein; Potassium channel KAT1
UniProt: Q5KTN5, Q39128
Ligands: FSC, SEP
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 11 distinct chains · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 C-1 protein	protein	239	83% helix, 0% strand	Q5KTN5
P, R, T, U	Potassium channel KAT1	protein	4	0% helix, 0% strand	Q39128
B	14-3-3 C-1 protein	protein	245	83% helix, 0% strand	Q5KTN5
Q, S, V	Potassium channel KAT1	protein	5	0% helix, 0% strand	Q39128
C	14-3-3 C-1 protein	protein	234	85% helix, 0% strand	Q5KTN5
D	14-3-3 C-1 protein	protein	236	85% helix, 0% strand	Q5KTN5
E	14-3-3 C-1 protein	protein	238	81% helix, 0% strand	Q5KTN5
F	14-3-3 C-1 protein	protein	237	84% helix, 0% strand	Q5KTN5
G	14-3-3 C-1 protein	protein	234	81% helix, 0% strand	Q5KTN5
H	14-3-3 C-1 protein	protein	213	85% helix, 0% strand	Q5KTN5
W	Potassium channel KAT1	protein	1	0% helix, 0% strand	Q39128

Ligands and binding sites

FSC · Fusicoccin · ligand · 7 copies · chains A, P, B, Q, C, R, D, S, E, T, F, U, G, V
SEP · Phosphoserine · ligand · chains H, W

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1103	0.80	0.82	77	FSC
2	1019	0.80	0.81	86	FSC
3	327	0.69	0.83	42	empty
4	745	0.67	0.75	69	empty
5	698	0.67	0.75	101	SEP

Interfaces

19 interfaces between chains.

A–B · 1296 Å² buried · 18 hydrogen bonds · protein-protein
E–F · 1284 Å² buried · 13 hydrogen bonds · protein-protein
D–E · 1216 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 1155 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 1144 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 modified, 1 covalent (phosphorylation, covalent ligand).

Compared structures

5NWK · 14-3-3c in complex with CPP and fusicoccin · the same entry in another collection · chain H against H, 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 Q5KTN5
Every structure of UniProt Q39128
Elsewhere: RCSB PDB 5NWK · PDBe 5NWK · UniProt Q5KTN5 · UniProt Q39128

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