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Structure of the P. aeruginosa exoy-F-actin complex

Analyse Structure of the P. aeruginosa exoy-F-actin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P1G
Type: protein
Length: 3,625 residues
Chains: 15
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,ADENYLATE cyclase exoy; Actin, alpha…
UniProt: Q9I1S4, P68135
Ligands: GH3, ADP, MG, PO4
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 3 distinct chains · 36% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
M, K, L, N, O	MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,ADENYLATE cyclase exoy	protein	347	32% helix, 17% strand	Q9I1S4
C, A, B, D, E	Actin, alpha skeletal muscle	protein	371	41% helix, 20% strand	P68135
H, F, G, I, J	Phalloidin	protein	7	0% helix, 14% strand	—

Ligands and binding sites

GH3 · 3'-deoxy-guanosine-5'-triphosphate · ligand · 5 copies · chains M, K, L, N, O
ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains C, A, B, D, E
MG · Magnesium ion · metal · 10 copies · chains M, C, K, A, L, B, N, D, O, E
PO4 · Phosphate ion · ion · 5 copies · chains C, A, B, D, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	682	0.84	0.88	72	empty
2	480	0.82	0.89	59	empty
3	453	0.81	0.89	51	empty
4	306	0.80	0.91	53	MG, ADP, PO4
5	662	0.78	0.83	94	MG, ADP, PO4

Interfaces

28 interfaces between chains.

N–D · 1621 Å² buried · 23 hydrogen bonds · protein-protein
O–E · 1617 Å² buried · 23 hydrogen bonds · protein-protein
M–C · 1617 Å² buried · 23 hydrogen bonds · protein-protein
K–A · 1614 Å² buried · 23 hydrogen bonds · protein-protein
L–B · 1612 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified, 5 d-amino (D-amino acid, hydroxylation, nonstandard).

Compared structures

7P1G · Structure of the P. aeruginosa ExoY-F-actin complex · the same entry in another collection · chain J against J, 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 Q9I1S4
Every structure of UniProt P68135
Elsewhere: RCSB PDB 7P1G · PDBe 7P1G · UniProt Q9I1S4 · UniProt P68135

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