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Structure of the human MSL3 chromo-barrel domain at 2.5 ångström resolution

Analyse Structure of the human MSL3 chromo-barrel domain at 2.5 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OB9
Type: protein
Length: 436 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Male-specific lethal 3-like 1 (drosophila), isoform CRA_C
UniProt: A6NHW8
Ligands: SO4
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 5 distinct chains · 24% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Male-specific lethal 3-like 1 (drosophila), isoform CRA_C	protein	89	22% helix, 38% strand	A6NHW8
B	Male-specific lethal 3-like 1 (drosophila), isoform CRA_C	protein	87	24% helix, 37% strand	A6NHW8
C	Male-specific lethal 3-like 1 (drosophila), isoform CRA_C	protein	88	24% helix, 39% strand	A6NHW8
D	Male-specific lethal 3-like 1 (drosophila), isoform CRA_C	protein	93	23% helix, 37% strand	A6NHW8
E	Male-specific lethal 3-like 1 (drosophila), isoform CRA_C	protein	79	27% helix, 38% strand	A6NHW8

Ligands and binding sites

SO4 · Sulfate ion · ion · 17 copies · chains A, B, C, D, E
NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 3 copies · chains A, D, 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, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	872	0.80	0.82	86	empty
2	505	0.73	0.81	46	empty
3	79	0.55	0.86	11	SO4
4	71	0.51	0.84	10	NHE
5	57	0.38	0.79	8	empty

Interfaces

6 interfaces between chains.

A–B · 692 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 623 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 422 Å² buried · 6 hydrogen bonds · protein-protein
B–E · 374 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 356 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3OB9 · Structure of the human MSL3 chromo-barrel domain at 2.5 Angstrom resolution · 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 A6NHW8
Elsewhere: RCSB PDB 3OB9 · PDBe 3OB9 · UniProt A6NHW8

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