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Crystal structure of the type one membrane protein MIX1 from leishmania

Analyse Crystal structure of the type one membrane protein MIX1 from leishmania in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HA4
Type: protein
Length: 936 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MIX1
UniProt: Q4QI49
Ligands: CO3
Pockets: 7 · best druggability 0.79

Structure

x-ray diffraction · 8 distinct chains · 67% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MIX1	protein	127	67% helix, 0% strand	Q4QI49
B	MIX1	protein	120	64% helix, 0% strand	Q4QI49
C	MIX1	protein	113	65% helix, 0% strand	Q4QI49
D	MIX1	protein	114	65% helix, 0% strand	Q4QI49
E	MIX1	protein	111	67% helix, 0% strand	Q4QI49
F	MIX1	protein	129	68% helix, 0% strand	Q4QI49
G	MIX1	protein	113	67% helix, 0% strand	Q4QI49
H	MIX1	protein	109	69% helix, 0% strand	Q4QI49

Ligands and binding sites

CO3 · Carbonate ion · ion · chains D

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

Pockets

7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	903	0.79	0.82	98	empty
2	100	0.69	0.92	20	empty
3	73	0.66	0.93	23	empty
4	211	0.58	0.80	32	empty
5	189	0.57	0.80	35	empty

Interfaces

10 interfaces between chains.

A–E · 1209 Å² buried · 9 hydrogen bonds · protein-protein
C–G · 1209 Å² buried · 13 hydrogen bonds · protein-protein
B–D · 1162 Å² buried · 15 hydrogen bonds · protein-protein
F–H · 1136 Å² buried · 10 hydrogen bonds · protein-protein
C–F · 483 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3HA4 · Crystal structure of the type one membrane protein MIX1 from Leishmania · 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 Q4QI49
Elsewhere: RCSB PDB 3HA4 · PDBe 3HA4 · UniProt Q4QI49

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