Research workbench

Wzz dodecamer fitted by mdff to the wzz experimental MAP from cryo-EM

Analyse Wzz dodecamer fitted by mdff to the wzz experimental MAP from cryo-EM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NBZ
Type: protein
Length: 2,844 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wzzb
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 60% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Wzzb	protein	237	60% helix, 10% strand	—

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	930	0.78	0.80	110	empty
2	1187	0.78	0.80	130	empty
3	572	0.77	0.84	83	empty
4	1144	0.76	0.78	110	empty
5	883	0.74	0.78	72	empty

Interfaces

12 interfaces between chains.

J–K · 2077 Å² buried · 25 hydrogen bonds · protein-protein
A–L · 2029 Å² buried · 30 hydrogen bonds · protein-protein
G–H · 1962 Å² buried · 24 hydrogen bonds · protein-protein
E–F · 1949 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 1906 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5NBZ · Wzz dodecamer fitted by MDFF to the Wzz experimental map from cryo-EM · 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
Elsewhere: RCSB PDB 5NBZ · PDBe 5NBZ

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