Research workbench

Yaxab pore complex

Analyse Yaxab pore complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EL1
Type: protein
Length: 6,830 residues
Chains: 20
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Yaxa; Yaxb
UniProt: A0A0T9S5R5, A1JM52
Pockets: 20 · best druggability 0.77

Structure

electron microscopy · 2 distinct chains · 81% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E, A, B, C, D, F, G, H, I, J	Yaxa	protein	351	84% helix, 1% strand	A0A0T9S5R5
O, K, L, M, N, P, Q, R, S, T	Yaxb	protein	332	78% helix, 0% strand	A1JM52

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	999	0.77	0.80	102	empty
2	386	0.76	0.86	58	empty
3	409	0.76	0.85	60	empty
4	976	0.76	0.78	94	empty
5	82	0.75	0.97	24	empty

Interfaces

40 interfaces between chains.

E–O · 2528 Å² buried · 27 hydrogen bonds · protein-protein
F–P · 2509 Å² buried · 28 hydrogen bonds · protein-protein
I–S · 2467 Å² buried · 22 hydrogen bonds · protein-protein
C–M · 2456 Å² buried · 25 hydrogen bonds · protein-protein
A–K · 2438 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

6EL1 · YaxAB pore complex · the same entry in another collection · chain E against E, 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 A0A0T9S5R5
Every structure of UniProt A1JM52
Elsewhere: RCSB PDB 6EL1 · PDBe 6EL1 · UniProt A0A0T9S5R5 · UniProt A1JM52

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