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ALP12 filament structure

Analyse ALP12 filament structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4APW
Type: protein
Length: 5,168 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALP12
UniProt: Q89A01
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	ALP12	protein	323	30% helix, 26% strand	Q89A01

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	983	0.81	0.82	120	empty
2	829	0.79	0.82	99	empty
3	1066	0.79	0.81	115	empty
4	1161	0.79	0.81	129	empty
5	799	0.79	0.82	104	empty

Interfaces

33 interfaces between chains.

K–L · 1340 Å² buried · 91 hydrogen bonds · protein-protein
F–G · 1337 Å² buried · 91 hydrogen bonds · protein-protein
E–F · 1337 Å² buried · 91 hydrogen bonds · protein-protein
G–H · 1336 Å² buried · 91 hydrogen bonds · protein-protein
J–K · 1334 Å² buried · 91 hydrogen bonds · protein-protein

Compared structures

4APW · Alp12 filament structure · 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 Q89A01
Elsewhere: RCSB PDB 4APW · PDBe 4APW · UniProt Q89A01

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