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Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of smc atpases.

Analyse Structural biochemistry of ATP-driven dimerization and DNA stimulated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XEX
Type: protein
Length: 327 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Smc protein
Ligands: ATP, MG
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Smc protein	protein	166	27% helix, 29% strand	—
B	Smc protein	protein	161	43% helix, 22% strand	—

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A, B
MG · Magnesium ion · metal · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	280	0.61	0.79	30	empty
2	139	0.54	0.80	17	empty
3	74	0.35	0.76	15	empty
4	51	0.26	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 2727 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

1XEX · Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1XEX · PDBe 1XEX

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