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Crystal structure of ATG101-ATG13HORMA

Analyse Crystal structure of ATG101-ATG13HORMA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XV4
Type: protein
Length: 3,124 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Autophagy-related protein 13; Autophagy-related protein 101
UniProt: O75143, Q9BSB4
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 6 distinct chains · 33% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E, G, I, K, O	Autophagy-related protein 13	protein	182	35% helix, 29% strand	O75143
B, D, F, J, P	Autophagy-related protein 101	protein	207	32% helix, 31% strand	Q9BSB4
C, M	Autophagy-related protein 13	protein	183	35% helix, 28% strand	O75143
H	Autophagy-related protein 101	protein	210	32% helix, 32% strand	Q9BSB4
L	Autophagy-related protein 101	protein	209	31% helix, 33% strand	Q9BSB4
N	Autophagy-related protein 101	protein	212	32% helix, 32% strand	Q9BSB4

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	873	0.80	0.82	102	empty
2	1198	0.74	0.77	106	empty
3	1149	0.69	0.74	81	empty
4	633	0.68	0.77	73	empty
5	246	0.68	0.84	35	empty

Interfaces

26 interfaces between chains.

G–H · 1365 Å² buried · 30 hydrogen bonds · protein-protein
M–N · 1354 Å² buried · 27 hydrogen bonds · protein-protein
I–J · 1350 Å² buried · 30 hydrogen bonds · protein-protein
K–L · 1346 Å² buried · 22 hydrogen bonds · protein-protein
A–B · 1339 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

5XV4 · Crystal structure of ATG101-ATG13HORMA · the same entry in another collection · chain K against K, 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 O75143
Every structure of UniProt Q9BSB4
Elsewhere: RCSB PDB 5XV4 · PDBe 5XV4 · UniProt O75143 · UniProt Q9BSB4

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