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Crystal structure of the human MST2 sarah homodimer

Analyse Crystal structure of the human MST2 sarah homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OH9
Type: protein
Length: 101 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase 3
EC: 2.7.11.1
UniProt: Q13188

Structure

x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1)	protein	51	84% helix, 0% strand	Q13188
B	SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1)	protein	50	86% helix, 0% strand	Q13188

Interfaces

1 interface between chains.

A–B · 1576 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

4OH9 · Crystal Structure of the human MST2 SARAH homodimer · the same entry in another collection · chain A against A, TM-score 1.00
Q13188 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase 3 (Q13188) · a predicted model of the same protein · chain A against A, TM-score 0.72

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 Q13188
Elsewhere: RCSB PDB 4OH9 · PDBe 4OH9 · UniProt Q13188

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