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Complex of LATS1 and phosphomimetic MOB1B

Analyse Complex of LATS1 and phosphomimetic MOB1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5B6B
Type: protein
Length: 1,999 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mob kinase activator 1B; SERINE/THREONINE-protein kinase LATS1
EC: 2.7.11.1
UniProt: Q8BPB0, Q8BYR2
Ligands: ZN, CL
Pockets: 20 · best druggability 0.84

Structure

x-ray diffraction · 15 distinct chains · 63% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mob kinase activator 1B	protein	182	55% helix, 2% strand	Q8BPB0
J	SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1)	protein	71	83% helix, 0% strand	Q8BYR2
B	Mob kinase activator 1B	protein	189	54% helix, 2% strand	Q8BPB0
C, E	SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1)	protein	71	82% helix, 0% strand	Q8BYR2
D	Mob kinase activator 1B	protein	177	57% helix, 1% strand	Q8BPB0
F	Mob kinase activator 1B	protein	183	58% helix, 2% strand	Q8BPB0
G	SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1)	protein	74	78% helix, 0% strand	Q8BYR2
H	Mob kinase activator 1B	protein	184	59% helix, 2% strand	Q8BPB0
I	SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1)	protein	72	81% helix, 0% strand	Q8BYR2
K	Mob kinase activator 1B	protein	180	53% helix, 2% strand	Q8BPB0
L	SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1)	protein	72	81% helix, 0% strand	Q8BYR2
M	Mob kinase activator 1B	protein	173	55% helix, 1% strand	Q8BPB0
N	SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1)	protein	65	86% helix, 0% strand	Q8BYR2
O	Mob kinase activator 1B	protein	170	56% helix, 1% strand	Q8BPB0
P	SERINE/THREONINE-protein kinase LATS1 (EC 2.7.11.1)	protein	65	85% helix, 0% strand	Q8BYR2

Ligands and binding sites

ZN · Zinc ion · metal · 8 copies · chains A, B, D, F, H, K, M, O
CL · Chloride ion · ion · 7 copies · chains A, B, D, F, H, K, M

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	610	0.84	0.89	81	empty
2	1005	0.80	0.81	60	empty
3	718	0.80	0.83	61	empty
4	843	0.79	0.82	66	empty
5	646	0.70	0.78	62	empty

Interfaces

32 interfaces between chains.

F–G · 1883 Å² buried · 25 hydrogen bonds · protein-protein
A–J · 1816 Å² buried · 17 hydrogen bonds · protein-protein
K–L · 1686 Å² buried · 19 hydrogen bonds · protein-protein
H–I · 1552 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 1470 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5B6B · Complex of LATS1 and phosphomimetic MOB1b · the same entry in another collection · chain K against K, 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 Q8BPB0
Every structure of UniProt Q8BYR2
Elsewhere: RCSB PDB 5B6B · PDBe 5B6B · UniProt Q8BPB0 · UniProt Q8BYR2

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