MolNFT v1 · #80350 · protein

1.92 ångström resolution crystal structure of the full-length spcu in complex with full-length exou from the type III secretion system of pseudomonas aeruginosa

3TU3 · Exou chaperone: “1.92 ångström resolution crystal structure of the full-length spcu in complex with full-length exou from the…”. X-ray diffraction, 10 pockets (best druggability 0.72). MolNFT v1 #80350 on GenesisL1: 3D structure…

PDB: 3TU3
Type: protein
Length: 645 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exou chaperone; Exou
UniProt: O66100, O34208
Pockets: 10 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exou chaperone	protein	119	31% helix, 29% strand	O66100
B	Exou	protein	526	56% helix, 13% strand	O34208

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	926	0.72	0.76	81	empty
2	69	0.57	0.88	17	empty
3	264	0.52	0.75	39	empty
4	56	0.42	0.82	13	empty
5	69	0.38	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 1556 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

3TU3 · 1.92 Angstrom resolution crystal structure of the full-length SpcU in complex with… · 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 O66100
Every structure of UniProt O34208
Elsewhere: RCSB PDB 3TU3 · PDBe 3TU3 · UniProt O66100 · UniProt O34208

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