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Crystal structure of dotm cytoplasmic domain (residues 153-380),R217E

Analyse Crystal structure of dotm cytoplasmic domain (residues 153-380),R217E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EXE
Type: protein
Length: 442 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Icmp (dotm)
UniProt: Q5ZYC7
Pockets: 5 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Icmp (dotm)	protein	219	60% helix, 3% strand	Q5ZYC7
B	Icmp (dotm)	protein	223	62% helix, 3% strand	Q5ZYC7

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · chains A, B
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	179	0.46	0.75	29	empty
2	53	0.37	0.80	16	empty
3	64	0.37	0.78	16	empty
4	63	0.33	0.76	17	empty
5	52	0.25	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 872 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6EXE · Crystal structure of DotM cytoplasmic domain (residues 153-380),R217E · the same entry in another collection · chain A against A, 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 Q5ZYC7
Elsewhere: RCSB PDB 6EXE · PDBe 6EXE · UniProt Q5ZYC7

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