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Crystal structure of FTSZ:MCIZ complex from bacillus subtilis

Analyse Crystal structure of FTSZ:MCIZ complex from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4U39
Type: protein
Length: 2,766 residues
Chains: 18
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz; Cell division factor
UniProt: P17865, L8EBJ9
Ligands: PO4
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 18 distinct chains · 47% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	294	45% helix, 25% strand	P17865
B	Cell division protein ftsz	protein	289	46% helix, 25% strand	P17865
C	Cell division protein ftsz	protein	288	47% helix, 25% strand	P17865
D	Cell division protein ftsz	protein	280	46% helix, 24% strand	P17865
E	Cell division protein ftsz	protein	286	46% helix, 25% strand	P17865
F	Cell division protein ftsz	protein	284	45% helix, 24% strand	P17865
G	Cell division protein ftsz	protein	279	47% helix, 24% strand	P17865
H	Cell division protein ftsz	protein	269	48% helix, 24% strand	P17865
I	Cell division protein ftsz	protein	270	46% helix, 23% strand	P17865
J	Cell division factor	protein	36	50% helix, 33% strand	L8EBJ9
K	Cell division factor	protein	15	53% helix, 13% strand	L8EBJ9
L	Cell division factor	protein	30	60% helix, 23% strand	L8EBJ9
M	Cell division factor	protein	25	68% helix, 8% strand	L8EBJ9
N	Cell division factor	protein	27	63% helix, 15% strand	L8EBJ9
O	Cell division factor	protein	28	43% helix, 25% strand	L8EBJ9
P	Cell division factor	protein	21	67% helix, 14% strand	L8EBJ9
Q	Cell division factor	protein	27	48% helix, 22% strand	L8EBJ9
R	Cell division factor	protein	18	56% helix, 17% strand	L8EBJ9

Ligands and binding sites

PO4 · Phosphate ion · ion · 16 copies · chains A, B, G, C, E, D, F, H, I

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

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	841	0.80	0.83	115	PO4
2	639	0.80	0.85	84	PO4
3	146	0.69	0.89	42	empty
4	92	0.59	0.87	29	empty
5	149	0.57	0.82	28	empty

Interfaces

29 interfaces between chains.

E–I · 1252 Å² buried · 15 hydrogen bonds · protein-protein
F–H · 1234 Å² buried · 12 hydrogen bonds · protein-protein
A–J · 1044 Å² buried · 17 hydrogen bonds · protein-protein
F–O · 867 Å² buried · 15 hydrogen bonds · protein-protein
E–N · 864 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

4U39 · Crystal Structure of FtsZ:MciZ Complex from Bacillus subtilis · the same entry in another collection · chain K against K, 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 P17865
Every structure of UniProt L8EBJ9
Elsewhere: RCSB PDB 4U39 · PDBe 4U39 · UniProt P17865 · UniProt L8EBJ9

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