MolNFT v1 · #141260 · protein

Cryo-EM structure of methanoccus maripaludis archaellum

5Z1L · Flagellin: “Cryo-EM structure of methanoccus maripaludis archaellum”. Electron microscopy, 20 pockets (best druggability 0.86). MolNFT v1 #141260 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5Z1L
Type: protein
Length: 3,582 residues
Chains: 18
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellin
UniProt: Q6LWP3
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 25% helix, 29% 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, Q, R	Flagellin	protein	199	25% helix, 29% strand	Q6LWP3

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	642	0.86	0.90	94	empty
2	371	0.80	0.89	66	empty
3	362	0.80	0.89	56	empty
4	407	0.79	0.88	60	empty
5	401	0.79	0.88	54	empty

Interfaces

65 interfaces between chains.

G–H · 1472 Å² buried · 8 hydrogen bonds · protein-protein
A–R · 1466 Å² buried · 9 hydrogen bonds · protein-protein
L–O · 1458 Å² buried · 9 hydrogen bonds · protein-protein
A–Q · 1451 Å² buried · 9 hydrogen bonds · protein-protein
E–P · 1451 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5Z1L · Cryo-EM structure of Methanoccus maripaludis archaellum · 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 Q6LWP3
Elsewhere: RCSB PDB 5Z1L · PDBe 5Z1L · UniProt Q6LWP3

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